Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P06612

- TOP1_ECOLI

UniProt

P06612 - TOP1_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

DNA topoisomerase 1

Gene

topA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiP06612.
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_dom.
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

        10         20         30         40         50
MGKALVIVES PAKAKTINKY LGSDYVVKSS VGHIRDLPTS GSAAKKSADS
60 70 80 90 100
TSTKTAKKPK KDERGALVNR MGVDPWHNWE AHYEVLPGKE KVVSELKQLA
110 120 130 140 150
EKADHIYLAT DLDREGEAIA WHLREVIGGD DARYSRVVFN EITKNAIRQA
160 170 180 190 200
FNKPGELNID RVNAQQARRF MDRVVGYMVS PLLWKKIARG LSAGRVQSVA
210 220 230 240 250
VRLVVERERE IKAFVPEEFW EVDASTTTPS GEALALQVTH QNDKPFRPVN
260 270 280 290 300
KEQTQAAVSL LEKARYSVLE REDKPTTSKP GAPFITSTLQ QAASTRLGFG
310 320 330 340 350
VKKTMMMAQR LYEAGYITYM RTDSTNLSQD AVNMVRGYIS DNFGKKYLPE
360 370 380 390 400
SPNQYASKEN SQEAHEAIRP SDVNVMAESL KDMEADAQKL YQLIWRQFVA
410 420 430 440 450
CQMTPAKYDS TTLTVGAGDF RLKARGRILR FDGWTKVMPA LRKGDEDRIL
460 470 480 490 500
PAVNKGDALT LVELTPAQHF TKPPARFSEA SLVKELEKRG IGRPSTYASI
510 520 530 540 550
ISTIQDRGYV RVENRRFYAE KMGEIVTDRL EENFRELMNY DFTAQMENSL
560 570 580 590 600
DQVANHEAEW KAVLDHFFSD FTQQLDKAEK DPEEGGMRPN QMVLTSIDCP
610 620 630 640 650
TCGRKMGIRT ASTGVFLGCS GYALPPKERC KTTINLVPEN EVLNVLEGED
660 670 680 690 700
AETNALRAKR RCPKCGTAMD SYLIDPKRKL HVCGNNPTCD GYEIEEGEFR
710 720 730 740 750
IKGYDGPIVE CEKCGSEMHL KMGRFGKYMA CTNEECKNTR KILRNGEVAP
760 770 780 790 800
PKEDPVPLPE LPCEKSDAYF VLRDGAAGVF LAANTFPKSR ETRAPLVEEL
810 820 830 840 850
YRFRDRLPEK LRYLADAPQQ DPEGNKTMVR FSRKTKQQYV SSEKDGKATG
860
WSAFYVDGKW VEGKK
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.
InParanoidi P06612.
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_dom.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 157 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