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P06612

- TOP1_ECOLI

UniProt

P06612 - TOP1_ECOLI

Protein

DNA topoisomerase 1

Gene

topA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.3 PublicationsUniRule annotation

    Catalytic activityi

    ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.4 PublicationsUniRule annotation

    Cofactori

    Magnesium. Binds two Mg2+ ions per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn2+ and Ca2+.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi9 – 91Magnesium 1; catalyticUniRule annotation
    Sitei33 – 331Interaction with DNA
    Metal bindingi111 – 1111Magnesium 1; catalyticCurated
    Metal bindingi111 – 1111Magnesium 2Curated
    Metal bindingi113 – 1131Magnesium 2Curated
    Sitei168 – 1681Interaction with DNA
    Sitei169 – 1691Interaction with DNA
    Sitei172 – 1721Interaction with DNA
    Sitei177 – 1771Interaction with DNA
    Sitei184 – 1841Interaction with DNA
    Active sitei319 – 3191O-(5'-phospho-DNA)-tyrosine intermediate3 PublicationsUniRule annotation
    Sitei321 – 3211Interaction with DNA
    Sitei507 – 5071Interaction with DNA

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri599 – 63032C4-type 1Add
    BLAST
    Zinc fingeri662 – 68928C4-type 2Add
    BLAST
    Zinc fingeri711 – 73626C4-type 3Add
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. DNA topoisomerase activity Source: EcoCyc
    3. DNA topoisomerase type I activity Source: EcoCyc
    4. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: InterPro
    5. magnesium ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. DNA strand elongation Source: EcoCyc
    2. DNA topological change Source: EcoliWiki

    Keywords - Molecular functioni

    Isomerase, Topoisomerase

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11013-MONOMER.
    ECOL316407:JW1266-MONOMER.
    MetaCyc:EG11013-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA topoisomerase 1UniRule annotation (EC:5.99.1.2UniRule annotation)
    Alternative name(s):
    DNA topoisomerase IUniRule annotation
    Omega-protein
    Relaxing enzyme
    Swivelase
    Untwisting enzyme
    Gene namesi
    Name:topAUniRule annotation
    Synonyms:supX
    Ordered Locus Names:b1274, JW1266
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11013. topA.

    Subcellular locationi

    GO - Cellular componenti

    1. chromosome Source: InterPro

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi9 – 91E → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi9 – 91E → Q: No effect on DNA cleavage activity. 1 Publication
    Mutagenesisi111 – 1111D → A: Abolishes both magnesium binding and enzyme activity; when associated with A-113 and A-115. 1 Publication
    Mutagenesisi113 – 1131D → A: Abolishes both magnesium binding and enzyme activity; when associated with A-111 and A-115. 1 Publication
    Mutagenesisi115 – 1151E → A: Abolishes both magnesium binding and enzyme activity; when associated with A-111 and A-113. 1 Publication
    Mutagenesisi168 – 1681R → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi172 – 1721D → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi319 – 3191Y → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi321 – 3211R → A: Abolishes enzyme activity. 1 Publication
    Mutagenesisi321 – 3211R → K: No effect. 1 Publication
    Mutagenesisi365 – 3651H → A: No effect. 2 Publications
    Mutagenesisi365 – 3651H → R: Increases DNA binding affinity. 2 Publications
    Mutagenesisi496 – 4961T → A: No effect. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 865865DNA topoisomerase 1PRO_0000145147Add
    BLAST

    Proteomic databases

    PaxDbiP06612.
    PRIDEiP06612.

    Expressioni

    Gene expression databases

    GenevestigatoriP06612.

    Interactioni

    Subunit structurei

    Monomer.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    DIPiDIP-11011N.
    IntActiP06612. 68 interactions.
    MINTiMINT-1218330.
    STRINGi511145.b1274.

    Structurei

    Secondary structure

    1
    865
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Helixi11 – 188
    Beta strandi25 – 295
    Beta strandi35 – 373
    Helixi64 – 718
    Beta strandi72 – 743
    Turni75 – 795
    Turni87 – 893
    Helixi90 – 10112
    Beta strandi104 – 1085
    Helixi114 – 12714
    Helixi131 – 1333
    Beta strandi134 – 1363
    Helixi144 – 1529
    Helixi159 – 18628
    Helixi197 – 21317
    Beta strandi218 – 22710
    Beta strandi229 – 2313
    Beta strandi233 – 2419
    Helixi251 – 26313
    Beta strandi266 – 27813
    Helixi286 – 29712
    Helixi301 – 31313
    Beta strandi316 – 3183
    Helixi329 – 34214
    Helixi345 – 3473
    Beta strandi356 – 3583
    Beta strandi362 – 3643
    Helixi377 – 3793
    Helixi385 – 40117
    Beta strandi406 – 41712
    Beta strandi420 – 43112
    Helixi433 – 4375
    Beta strandi458 – 47013
    Helixi479 – 48810
    Turni494 – 4963
    Helixi497 – 50610
    Beta strandi509 – 5135
    Beta strandi516 – 5194
    Helixi521 – 53313
    Helixi535 – 5384
    Helixi540 – 55415
    Helixi560 – 57920
    Helixi582 – 5843
    Beta strandi755 – 7628
    Beta strandi764 – 7674
    Beta strandi769 – 7735
    Beta strandi776 – 7783
    Beta strandi780 – 7834
    Turni784 – 7874
    Helixi797 – 8026
    Turni803 – 8064
    Helixi812 – 8165
    Beta strandi827 – 8326
    Turni833 – 8364
    Beta strandi837 – 8426
    Beta strandi853 – 8553

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CY0X-ray2.45A1-597[»]
    1CY1X-ray2.30A1-597[»]
    1CY2X-ray2.30A1-597[»]
    1CY4X-ray2.55A1-597[»]
    1CY6X-ray2.50A1-597[»]
    1CY7X-ray2.40A1-597[»]
    1CY8X-ray2.45A1-597[»]
    1CY9X-ray1.80A/B214-477[»]
    1CYYX-ray2.15A/B214-477[»]
    1ECLX-ray1.90A1-597[»]
    1MW8X-ray1.90X1-592[»]
    1MW9X-ray1.67X1-592[»]
    1YUANMR-A745-865[»]
    3PWTX-ray1.90A1-596[»]
    3PX7X-ray2.30A1-595[»]
    ProteinModelPortaliP06612.
    SMRiP06612. Positions 2-619, 745-865.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06612.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 142140ToprimUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni192 – 1976Interaction with DNA

    Sequence similaritiesi

    Belongs to the type IA topoisomerase family.UniRule annotation
    Contains 1 Toprim domain.UniRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri599 – 63032C4-type 1Add
    BLAST
    Zinc fingeri662 – 68928C4-type 2Add
    BLAST
    Zinc fingeri711 – 73626C4-type 3Add
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0551.
    HOGENOMiHOG000004018.
    KOiK03168.
    OMAiVVECDKC.
    OrthoDBiEOG6S7XQ9.
    PhylomeDBiP06612.

    Family and domain databases

    Gene3Di1.10.460.10. 3 hits.
    2.70.20.10. 2 hits.
    3.40.50.140. 1 hit.
    HAMAPiMF_00952. Topoisom_1_prok.
    InterProiIPR000380. Topo_IA.
    IPR003601. Topo_IA_2.
    IPR023406. Topo_IA_AS.
    IPR013497. Topo_IA_cen.
    IPR013824. Topo_IA_cen_sub1.
    IPR013825. Topo_IA_cen_sub2.
    IPR023405. Topo_IA_core_domain.
    IPR003602. Topo_IA_DNA-bd.
    IPR013498. Topo_IA_Znf.
    IPR005733. TopoI_bac-type.
    IPR013263. TopoI_Znr_bac.
    IPR028612. Topoisom_1_IA.
    IPR006171. Toprim_domain.
    [Graphical view]
    PANTHERiPTHR11390. PTHR11390. 1 hit.
    PfamiPF08272. Topo_Zn_Ribbon. 2 hits.
    PF01131. Topoisom_bac. 1 hit.
    PF01751. Toprim. 1 hit.
    PF01396. zf-C4_Topoisom. 2 hits.
    [Graphical view]
    PRINTSiPR00417. PRTPISMRASEI.
    SMARTiSM00437. TOP1Ac. 1 hit.
    SM00436. TOP1Bc. 1 hit.
    SM00493. TOPRIM. 1 hit.
    [Graphical view]
    SUPFAMiSSF56712. SSF56712. 1 hit.
    TIGRFAMsiTIGR01051. topA_bact. 1 hit.
    PROSITEiPS00396. TOPOISOMERASE_I_PROK. 1 hit.
    PS50880. TOPRIM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06612-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGKALVIVES PAKAKTINKY LGSDYVVKSS VGHIRDLPTS GSAAKKSADS    50
    TSTKTAKKPK KDERGALVNR MGVDPWHNWE AHYEVLPGKE KVVSELKQLA 100
    EKADHIYLAT DLDREGEAIA WHLREVIGGD DARYSRVVFN EITKNAIRQA 150
    FNKPGELNID RVNAQQARRF MDRVVGYMVS PLLWKKIARG LSAGRVQSVA 200
    VRLVVERERE IKAFVPEEFW EVDASTTTPS GEALALQVTH QNDKPFRPVN 250
    KEQTQAAVSL LEKARYSVLE REDKPTTSKP GAPFITSTLQ QAASTRLGFG 300
    VKKTMMMAQR LYEAGYITYM RTDSTNLSQD AVNMVRGYIS DNFGKKYLPE 350
    SPNQYASKEN SQEAHEAIRP SDVNVMAESL KDMEADAQKL YQLIWRQFVA 400
    CQMTPAKYDS TTLTVGAGDF RLKARGRILR FDGWTKVMPA LRKGDEDRIL 450
    PAVNKGDALT LVELTPAQHF TKPPARFSEA SLVKELEKRG IGRPSTYASI 500
    ISTIQDRGYV RVENRRFYAE KMGEIVTDRL EENFRELMNY DFTAQMENSL 550
    DQVANHEAEW KAVLDHFFSD FTQQLDKAEK DPEEGGMRPN QMVLTSIDCP 600
    TCGRKMGIRT ASTGVFLGCS GYALPPKERC KTTINLVPEN EVLNVLEGED 650
    AETNALRAKR RCPKCGTAMD SYLIDPKRKL HVCGNNPTCD GYEIEEGEFR 700
    IKGYDGPIVE CEKCGSEMHL KMGRFGKYMA CTNEECKNTR KILRNGEVAP 750
    PKEDPVPLPE LPCEKSDAYF VLRDGAAGVF LAANTFPKSR ETRAPLVEEL 800
    YRFRDRLPEK LRYLADAPQQ DPEGNKTMVR FSRKTKQQYV SSEKDGKATG 850
    WSAFYVDGKW VEGKK 865
    Length:865
    Mass (Da):97,350
    Last modified:February 1, 1995 - v2
    Checksum:i8C13F767FE5B178C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti787 – 7871P → R in AAA23641. (PubMed:3032952)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04475 Genomic DNA. Translation: CAA28164.1.
    M15041 Genomic DNA. Translation: AAA23641.1.
    U00096 Genomic DNA. Translation: AAC74356.1.
    AP009048 Genomic DNA. Translation: BAA14811.1.
    PIRiE64875. ISECTP.
    RefSeqiNP_415790.1. NC_000913.3.
    YP_489542.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC74356; AAC74356; b1274.
    BAA14811; BAA14811; BAA14811.
    GeneIDi12930585.
    945862.
    KEGGiecj:Y75_p1248.
    eco:b1274.
    PATRICi32117806. VBIEscCol129921_1323.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04475 Genomic DNA. Translation: CAA28164.1 .
    M15041 Genomic DNA. Translation: AAA23641.1 .
    U00096 Genomic DNA. Translation: AAC74356.1 .
    AP009048 Genomic DNA. Translation: BAA14811.1 .
    PIRi E64875. ISECTP.
    RefSeqi NP_415790.1. NC_000913.3.
    YP_489542.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CY0 X-ray 2.45 A 1-597 [» ]
    1CY1 X-ray 2.30 A 1-597 [» ]
    1CY2 X-ray 2.30 A 1-597 [» ]
    1CY4 X-ray 2.55 A 1-597 [» ]
    1CY6 X-ray 2.50 A 1-597 [» ]
    1CY7 X-ray 2.40 A 1-597 [» ]
    1CY8 X-ray 2.45 A 1-597 [» ]
    1CY9 X-ray 1.80 A/B 214-477 [» ]
    1CYY X-ray 2.15 A/B 214-477 [» ]
    1ECL X-ray 1.90 A 1-597 [» ]
    1MW8 X-ray 1.90 X 1-592 [» ]
    1MW9 X-ray 1.67 X 1-592 [» ]
    1YUA NMR - A 745-865 [» ]
    3PWT X-ray 1.90 A 1-596 [» ]
    3PX7 X-ray 2.30 A 1-595 [» ]
    ProteinModelPortali P06612.
    SMRi P06612. Positions 2-619, 745-865.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-11011N.
    IntActi P06612. 68 interactions.
    MINTi MINT-1218330.
    STRINGi 511145.b1274.

    Proteomic databases

    PaxDbi P06612.
    PRIDEi P06612.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC74356 ; AAC74356 ; b1274 .
    BAA14811 ; BAA14811 ; BAA14811 .
    GeneIDi 12930585.
    945862.
    KEGGi ecj:Y75_p1248.
    eco:b1274.
    PATRICi 32117806. VBIEscCol129921_1323.

    Organism-specific databases

    EchoBASEi EB1006.
    EcoGenei EG11013. topA.

    Phylogenomic databases

    eggNOGi COG0551.
    HOGENOMi HOG000004018.
    KOi K03168.
    OMAi VVECDKC.
    OrthoDBi EOG6S7XQ9.
    PhylomeDBi P06612.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG11013-MONOMER.
    ECOL316407:JW1266-MONOMER.
    MetaCyc:EG11013-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P06612.
    PROi P06612.

    Gene expression databases

    Genevestigatori P06612.

    Family and domain databases

    Gene3Di 1.10.460.10. 3 hits.
    2.70.20.10. 2 hits.
    3.40.50.140. 1 hit.
    HAMAPi MF_00952. Topoisom_1_prok.
    InterProi IPR000380. Topo_IA.
    IPR003601. Topo_IA_2.
    IPR023406. Topo_IA_AS.
    IPR013497. Topo_IA_cen.
    IPR013824. Topo_IA_cen_sub1.
    IPR013825. Topo_IA_cen_sub2.
    IPR023405. Topo_IA_core_domain.
    IPR003602. Topo_IA_DNA-bd.
    IPR013498. Topo_IA_Znf.
    IPR005733. TopoI_bac-type.
    IPR013263. TopoI_Znr_bac.
    IPR028612. Topoisom_1_IA.
    IPR006171. Toprim_domain.
    [Graphical view ]
    PANTHERi PTHR11390. PTHR11390. 1 hit.
    Pfami PF08272. Topo_Zn_Ribbon. 2 hits.
    PF01131. Topoisom_bac. 1 hit.
    PF01751. Toprim. 1 hit.
    PF01396. zf-C4_Topoisom. 2 hits.
    [Graphical view ]
    PRINTSi PR00417. PRTPISMRASEI.
    SMARTi SM00437. TOP1Ac. 1 hit.
    SM00436. TOP1Bc. 1 hit.
    SM00493. TOPRIM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56712. SSF56712. 1 hit.
    TIGRFAMsi TIGR01051. topA_bact. 1 hit.
    PROSITEi PS00396. TOPOISOMERASE_I_PROK. 1 hit.
    PS50880. TOPRIM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete nucleotide sequence of the topA gene encoding Escherichia coli DNA topoisomerase I."
      Tse-Dinh Y.-C., Wang J.C.
      J. Mol. Biol. 191:321-331(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Lynch D.A., Wang J.C.
      Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "DNA sequences of the cysB regions of Salmonella typhimurium and Escherichia coli."
      Ostrowski J., Jagura-Burdzy G., Kredich N.M.
      J. Biol. Chem. 262:5999-6005(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 698-865.
    7. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    8. "Identification of active site residues in Escherichia coli DNA topoisomerase I."
      Chen S.J., Wang J.C.
      J. Biol. Chem. 273:6050-6056(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLU-9; TYR-319; ARG-321; HIS-365 AND THR-496, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE.
    9. "The acidic triad conserved in type IA DNA topoisomerases is required for binding of Mg(II) and subsequent conformational change."
      Zhu C.X., Tse-Dinh Y.C.
      J. Biol. Chem. 275:5318-5322(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-111; ASP-113 AND GLU-115, COFACTOR, FUNCTION, ENZYME MECHANISM, METAL-BINDING SITES, CATALYTIC ACTIVITY.
    10. "Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I."
      Lima C.D., Wang J.C., Mondragon A.
      Nature 367:138-146(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-597, PUTATIVE METAL-BINDING SITES, ACTIVE SITE.
    11. "Solution structure of the C-terminal single-stranded DNA-binding domain of Escherichia coli topoisomerase I."
      Yu L., Zhu C.-X., Tse-Dinh Y.-C., Fesik S.W.
      Biochemistry 34:7622-7628(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 745-865.
    12. "Conformational changes in E. coli DNA topoisomerase I."
      Feinberg H., Lima C.D., Mondragon A.
      Nat. Struct. Biol. 6:918-922(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 214-477.
    13. "Protein-nucleotide interactions in E. coli DNA topoisomerase I."
      Feinberg H., Changela A., Mondragon A.
      Nat. Struct. Biol. 6:961-968(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-597 IN COMPLEXES WITH NUCLEOTIDES.
    14. "Structure of a complex between E. coli DNA topoisomerase I and single-stranded DNA."
      Perry K., Mondragon A.
      Structure 11:1349-1358(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 1-592 OF MUTANT ARG-365 IN COMPLEX WITH SINGLE-STANDED DNA, MUTAGENESIS OF HIS-365, CATALYTIC ACTIVITY.
    15. "Crystal structure of a covalent intermediate in DNA cleavage and rejoining by Escherichia coli DNA topoisomerase I."
      Zhang Z., Cheng B., Tse-Dinh Y.C.
      Proc. Natl. Acad. Sci. U.S.A. 108:6939-6944(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-596 OF MUTANT ASN-111 IN COMPLEX WITH DNA, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR, MUTAGENESIS OF ARG-168 AND ASP-172, DNA-BINDING SITES, ENZYME MECHANISM.

    Entry informationi

    Entry nameiTOP1_ECOLI
    AccessioniPrimary (citable) accession number: P06612
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 156 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3