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P0ABD3

- BFR_ECOLI

UniProt

P0ABD3 - BFR_ECOLI

Protein

Bacterioferritin

Gene

bfr

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

    Iron-storage protein, whose ferroxidase center binds Fe2+ ions, oxidizes them by dioxygen to Fe3+, and participates in the subsequent Fe3+ oxide mineral core formation within the central cavity of the protein complex. The mineralized iron core can contain as many as 2700 iron atoms/24-meric molecule.2 Publications

    Catalytic activityi

    4 Fe2+ + 4 H+ + O2 = 4 Fe3+ + 2 H2O.3 Publications

    Cofactori

    Binds 1 heme B (iron-protoporphyrin IX) group per dimer.1 Publication
    Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center. In BFR, the ferroxidase center appears to function as a true di-iron catalytic cofactor, rather than as a pore for the transfer of iron into the central cavity, as found for eukaryotic ferritins.1 Publication

    Enzyme regulationi

    Iron oxidation is inhibited by Zn2+, which binds at the ferroxidase center with a higher affinity that Fe2+. The occupation of the ferroxidase center by Zn2+ also severely restricts the ability of BFR to form an iron core.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi18 – 181Iron 11 PublicationPROSITE-ProRule annotation
    Metal bindingi46 – 461Iron 31 PublicationPROSITE-ProRule annotation
    Metal bindingi50 – 501Iron 31 PublicationPROSITE-ProRule annotation
    Metal bindingi51 – 511Iron 11 PublicationPROSITE-ProRule annotation
    Metal bindingi51 – 511Iron 21 PublicationPROSITE-ProRule annotation
    Metal bindingi52 – 521Iron (heme axial ligand); shared with dimeric partner1 PublicationPROSITE-ProRule annotation
    Metal bindingi54 – 541Iron 11 PublicationPROSITE-ProRule annotation
    Metal bindingi94 – 941Iron 21 PublicationPROSITE-ProRule annotation
    Metal bindingi127 – 1271Iron 11 PublicationPROSITE-ProRule annotation
    Metal bindingi127 – 1271Iron 21 PublicationPROSITE-ProRule annotation
    Metal bindingi130 – 1301Iron 21 PublicationPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ferric iron binding Source: InterPro
    2. ferroxidase activity Source: UniProtKB-EC
    3. heme binding Source: EcoCyc
    4. identical protein binding Source: EcoCyc
    5. iron ion binding Source: EcoCyc
    6. oxidoreductase activity Source: EcoliWiki

    GO - Biological processi

    1. intracellular sequestering of iron ion Source: EcoCyc
    2. iron ion transport Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Iron storage

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10113-MONOMER.
    ECOL316407:JW3298-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bacterioferritin (EC:1.16.3.1)
    Short name:
    BFR
    Alternative name(s):
    Cytochrome b-1
    Cytochrome b-557
    Gene namesi
    Name:bfr
    Ordered Locus Names:b3336, JW3298
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10113. bfr.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi18 – 181E → A: Highly decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. 1 Publication
    Mutagenesisi31 – 311M → H or L: No loss of heme binding. 1 Publication
    Mutagenesisi46 – 461H → A: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired. 1 Publication
    Mutagenesisi50 – 501D → A: Fe(2+)-binding and single turnover oxidation at the ferroxidase center occur normally but iron mineralization within the cavity is significantly impaired. 1 Publication
    Mutagenesisi52 – 521M → H or L: Loss of heme binding. Is still capable of accumulating iron. 1 Publication
    Mutagenesisi86 – 861M → L: No loss of heme binding. 1 Publication
    Mutagenesisi127 – 1271E → Q: Decreased Fe(2+) oxidation activity. Is also affected in its ability to lay down an iron core. 1 Publication
    Mutagenesisi130 – 1301H → E: Decreased Fe(2+) oxidation activity. Is also severely restricted in its ability to lay down an iron core. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 158158BacterioferritinPRO_0000192592Add
    BLAST

    Proteomic databases

    PaxDbiP0ABD3.
    PRIDEiP0ABD3.

    Expressioni

    Gene expression databases

    GenevestigatoriP0ABD3.

    Interactioni

    Subunit structurei

    Homooligomer of 24 subunits, arranged as 12 dimers, that are packed together to form an approximately spherical molecule with a central cavity, in which large amounts of iron can be deposited as a ferric-oxy-hydroxide mineral core.7 Publications

    Protein-protein interaction databases

    DIPiDIP-36167N.
    IntActiP0ABD3. 2 interactions.
    STRINGi511145.b3336.

    Structurei

    Secondary structure

    1
    158
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 3430
    Helixi38 – 6427
    Helixi83 – 11028
    Helixi114 – 14431
    Helixi146 – 1516

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BCFX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
    1BFRX-ray2.94A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1-158[»]
    2HTNX-ray2.50A/B/C/D/E/F/G/H1-158[»]
    2VXIX-ray1.91A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
    2Y3QX-ray1.55A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
    3E1JX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
    3E1LX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
    3E1MX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
    3E1NX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
    3E1OX-ray2.95A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
    3E1PX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
    3E1QX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
    3E2CX-ray1.80A/B1-158[»]
    3GHQX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L1-158[»]
    ProteinModelPortaliP0ABD3.
    SMRiP0ABD3. Positions 1-157.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ABD3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 145145Ferritin-like diironPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the bacterioferritin family.Curated
    Contains 1 ferritin-like diiron domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2193.
    HOGENOMiHOG000262383.
    KOiK03594.
    OMAiCTRNTAV.
    OrthoDBiEOG6WDSKP.
    PhylomeDBiP0ABD3.

    Family and domain databases

    Gene3Di1.20.1260.10. 1 hit.
    InterProiIPR002024. Bacterioferritin.
    IPR009040. Ferritin-like_diiron.
    IPR009078. Ferritin-like_SF.
    IPR012347. Ferritin-rel.
    IPR008331. Ferritin_DPS_dom.
    [Graphical view]
    PfamiPF00210. Ferritin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002560. Bacterioferritin. 1 hit.
    PRINTSiPR00601. BACFERRITIN.
    SUPFAMiSSF47240. SSF47240. 1 hit.
    TIGRFAMsiTIGR00754. bfr. 1 hit.
    PROSITEiPS00549. BACTERIOFERRITIN. 1 hit.
    PS50905. FERRITIN_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0ABD3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGDTKVINY LNKLLGNELV AINQYFLHAR MFKNWGLKRL NDVEYHESID    50
    EMKHADRYIE RILFLEGLPN LQDLGKLNIG EDVEEMLRSD LALELDGAKN 100
    LREAIGYADS VHDYVSRDMM IEILRDEEGH IDWLETELDL IQKMGLQNYL 150
    QAQIREEG 158
    Length:158
    Mass (Da):18,495
    Last modified:October 25, 2005 - v1
    Checksum:iA6C86CE1CD8F865A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531K → M AA sequence (PubMed:2644932)Curated

    Mass spectrometryi

    Molecular mass is 18496±2 Da from positions 1 - 158. Determined by ESI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 73TKV → VKI in strain: ECOR 30.
    Natural varianti38 – 381K → M in strain: ECOR 30.
    Natural varianti57 – 571R → K in strain: ECOR 30.
    Natural varianti68 – 681L → I in strain: ECOR 30.
    Natural varianti78 – 781N → G in strain: ECOR 30.
    Natural varianti88 – 881R → Q in strain: ECOR 30.
    Natural varianti92 – 921A → R in strain: ECOR 30.
    Natural varianti96 – 961D → E in strain: ECOR 30.
    Natural varianti100 – 1001N → D in strain: ECOR 30.
    Natural varianti106 – 1061G → A in strain: ECOR 30.
    Natural varianti125 – 1251R → A in strain: ECOR 30.
    Natural varianti142 – 1443QKM → GKI in strain: ECOR 30.
    Natural varianti152 – 1587AQIREEG → SQIKVKD in strain: ECOR 30.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27176 mRNA. Translation: AAC13987.1.
    AF058450 Genomic DNA. Translation: AAC14288.1.
    U18997 Genomic DNA. Translation: AAA58133.1.
    U00096 Genomic DNA. Translation: AAC76361.1.
    AP009048 Genomic DNA. Translation: BAE77955.1.
    L28106 Genomic DNA. Translation: AAC36929.1.
    PIRiJV0032. FREC.
    RefSeqiNP_417795.1. NC_000913.3.
    YP_492096.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76361; AAC76361; b3336.
    BAE77955; BAE77955; BAE77955.
    GeneIDi12933472.
    947839.
    KEGGiecj:Y75_p3840.
    eco:b3336.
    PATRICi32122104. VBIEscCol129921_3429.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27176 mRNA. Translation: AAC13987.1 .
    AF058450 Genomic DNA. Translation: AAC14288.1 .
    U18997 Genomic DNA. Translation: AAA58133.1 .
    U00096 Genomic DNA. Translation: AAC76361.1 .
    AP009048 Genomic DNA. Translation: BAE77955.1 .
    L28106 Genomic DNA. Translation: AAC36929.1 .
    PIRi JV0032. FREC.
    RefSeqi NP_417795.1. NC_000913.3.
    YP_492096.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BCF X-ray 2.90 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
    1BFR X-ray 2.94 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1-158 [» ]
    2HTN X-ray 2.50 A/B/C/D/E/F/G/H 1-158 [» ]
    2VXI X-ray 1.91 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
    2Y3Q X-ray 1.55 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
    3E1J X-ray 2.70 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
    3E1L X-ray 2.50 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
    3E1M X-ray 2.70 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
    3E1N X-ray 2.80 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
    3E1O X-ray 2.95 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
    3E1P X-ray 2.40 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
    3E1Q X-ray 2.60 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
    3E2C X-ray 1.80 A/B 1-158 [» ]
    3GHQ X-ray 2.70 A/B/C/D/E/F/G/H/I/J/K/L 1-158 [» ]
    ProteinModelPortali P0ABD3.
    SMRi P0ABD3. Positions 1-157.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36167N.
    IntActi P0ABD3. 2 interactions.
    STRINGi 511145.b3336.

    Proteomic databases

    PaxDbi P0ABD3.
    PRIDEi P0ABD3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76361 ; AAC76361 ; b3336 .
    BAE77955 ; BAE77955 ; BAE77955 .
    GeneIDi 12933472.
    947839.
    KEGGi ecj:Y75_p3840.
    eco:b3336.
    PATRICi 32122104. VBIEscCol129921_3429.

    Organism-specific databases

    EchoBASEi EB0111.
    EcoGenei EG10113. bfr.

    Phylogenomic databases

    eggNOGi COG2193.
    HOGENOMi HOG000262383.
    KOi K03594.
    OMAi CTRNTAV.
    OrthoDBi EOG6WDSKP.
    PhylomeDBi P0ABD3.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10113-MONOMER.
    ECOL316407:JW3298-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0ABD3.
    PROi P0ABD3.

    Gene expression databases

    Genevestigatori P0ABD3.

    Family and domain databases

    Gene3Di 1.20.1260.10. 1 hit.
    InterProi IPR002024. Bacterioferritin.
    IPR009040. Ferritin-like_diiron.
    IPR009078. Ferritin-like_SF.
    IPR012347. Ferritin-rel.
    IPR008331. Ferritin_DPS_dom.
    [Graphical view ]
    Pfami PF00210. Ferritin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002560. Bacterioferritin. 1 hit.
    PRINTSi PR00601. BACFERRITIN.
    SUPFAMi SSF47240. SSF47240. 1 hit.
    TIGRFAMsi TIGR00754. bfr. 1 hit.
    PROSITEi PS00549. BACTERIOFERRITIN. 1 hit.
    PS50905. FERRITIN_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing, and mapping of the bacterioferritin gene (bfr) of Escherichia coli K-12."
      Andrews S.C., Harrison P.M., Guest J.R.
      J. Bacteriol. 171:3940-3947(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Noorani S.M., Lindahl L., Zengel J.M.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ECOR 30.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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.
    5. "Amino acid sequence of the bacterioferritin (cytochrome b1) of Escherichia coli-K12."
      Andrews S.C., Smith J.M.A., Guest J.R., Harrison P.M.
      Biochem. Biophys. Res. Commun. 158:489-496(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-87.
      Strain: K12.
    6. "Escherichia coli contains a set of genes homologous to those involved in protein secretion, DNA uptake and the assembly of type-4 fimbriae in other bacteria."
      Whitchurch C.B., Mattick J.S.
      Gene 150:9-15(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-158.
      Strain: K12.
    7. "Site-directed replacement of the coaxial heme ligands of bacterioferritin generates heme-free variants."
      Andrews S.C., Le Brun N.E., Barynin V., Thomson A.J., Moore G.R., Guest J.R., Harrison P.M.
      J. Biol. Chem. 270:23268-23274(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: HEME-BINDING, MASS SPECTROMETRY, MUTAGENESIS OF MET-31; MET-52 AND MET-86.
      Strain: K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926.
    8. "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.
    9. "The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin."
      Yang X., Le Brun N.E., Thomson A.J., Moore G.R., Chasteen N.D.
      Biochemistry 39:4915-4923(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
    10. "Core formation in Escherichia coli bacterioferritin requires a functional ferroxidase center."
      Baaghil S., Lewin A., Moore G.R., Le Brun N.E.
      Biochemistry 42:14047-14056(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ROLE OF THE FERROXIDASE CENTER IN CORE FORMATION, CATALYTIC ACTIVITY, ENZYME REGULATION, MUTAGENESIS OF GLU-18; GLU-127 AND HIS-130.
    11. "Structure of a unique twofold symmetric haem-binding site."
      Frolow F., Kalb A.J., Yariv J.
      Nat. Struct. Biol. 1:453-460(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH HEME AND MANGANESE IONS.
    12. "Structure of a monoclinic crystal form of cyctochrome b1 (bacterioferritin) from E. coli."
      Dautant A., Meyer J.-B., Yariv J., Precigoux G., Sweet R.M., Kalb A.J., Frolow F.
      Acta Crystallogr. D 54:16-24(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) IN COMPLEX WITH HEME AND MANGANESE IONS, SUBUNIT.
    13. "Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form."
      van Eerde A., Wolterink-van Loo S., van der Oost J., Dijkstra B.W.
      Acta Crystallogr. F 62:1061-1066(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH HEME; IRON AND ZINC IONS.
      Strain: B / BL21.
    14. "Monitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopy."
      Lawson T.L., Crow A., Lewin A., Yasmin S., Moore G.R., Le Brun N.E.
      Biochemistry 48:9031-9039(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANTS PHE-35 AND PHE-133 IN COMPLEX WITH HEME AND IRON IONS, CATALYTIC ACTIVITY, ENZYME REGULATION.
      Strain: K12 / JM109 / ATCC 53323.
    15. "Structural basis for iron mineralization by bacterioferritin."
      Crow A., Lawson T.L., Lewin A., Moore G.R., Le Brun N.E.
      J. Am. Chem. Soc. 131:6808-6813(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF METAL-FREE APOPROTEIN AND IN COMPLEXES WITH ZN(2+); FE(2+); FE(3+) AND HEME, COFACTOR, INTERNAL SURFACE IRON-BINDING SITE, MUTAGENESIS OF HIS-46 AND ASP-50, MECHANISM OF IRON MINERALIZATION.
      Strain: K12 / JM109 / ATCC 53323.
    16. "Structural and mechanistic studies of a stabilized subunit dimer variant of Escherichia coli bacterioferritin identify residues required for core formation."
      Wong S.G., Tom-Yew S.A., Lewin A., Le Brun N.E., Moore G.R., Murphy M.E., Mauk A.G.
      J. Biol. Chem. 284:18873-18881(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ARG-128/ARG-135 DIMER IN COMPLEX WITH HEME AND ZINC IONS.
    17. "The binding of haem and zinc in the 1.9 A X-ray structure of Escherichia coli bacterioferritin."
      Willies S.C., Isupov M.N., Garman E.F., Littlechild J.A.
      J. Biol. Inorg. Chem. 14:201-207(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH HEME AND ZINC IONS.
      Strain: B / BL21.
    18. "Monitoring and validating active site redox states in protein crystals."
      Antonyuk S.V., Hough M.A.
      Biochim. Biophys. Acta 1814:778-784(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH HEME.

    Entry informationi

    Entry nameiBFR_ECOLI
    AccessioniPrimary (citable) accession number: P0ABD3
    Secondary accession number(s): O68931, P11056, Q2M701
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: October 25, 2005
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The internal surface iron site that binds iron 3 is important for the mineralization phase but not for Fe2+ binding and oxidation at the ferroxidase center.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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

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