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http://purl.uniprot.org/citations/12657783http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12657783http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12657783http://www.w3.org/2000/01/rdf-schema#comment"The structure of dimeric cytochrome c(3) from the sulfate-reducing bacterium Desulfovibrio gigas, diDg, obtained by ab initio methods was further refined to 1.2 A resolution, giving final reliability factors of R(free) = 14.8% and R = 12.4%. This cytochrome is a dimer of tetraheme cytochrome c(3) molecules covalently linked by two solvent-accessible disulfide bridges, a characteristic unique to members of the cytochrome c(3) superfamily. Anisotropic analysis using the semi-rigid TLS method shows different behaviour for analogous loops in each monomer arising from their different packing environments. A detailed sequence and structural comparison with all other known cytochrome c(3) domains in single- and multi-domain cytochromes c(3) shows the presence of structurally conserved regions in this family, despite the high variability of the amino-acid sequence. An internal water molecule is conserved in a common structural arrangement in all c(3) tetraheme domains, indicating a probable electron-transfer pathway between hemes I and II. Unique features of diDg are an internal methionine residue close to heme I and to one of the axial ligands of heme III, where all other structures of the cytochrome c(3) superfamily have a phenylalanine, and a rather unusual CXXXCH heme-binding motif only found so far in this cytochrome."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.org/dc/terms/identifier"doi:10.1107/S090744490300194X"xsd:string
http://purl.uniprot.org/citations/12657783http://purl.org/dc/terms/identifier"doi:10.1107/s090744490300194x"xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/author"Aragao D."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/author"Aragao D."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/author"Carrondo M.A."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/author"Carrondo M.A."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/author"Frazao C."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/author"Frazao C."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/author"LeGall J."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/author"LeGall J."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/author"Sieker L."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/author"Sieker L."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/author"Sheldrick G.M."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/author"Sheldrick G.M."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/name"Acta Crystallogr. D"xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/name"Acta Crystallogr D Biol Crystallogr"xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/pages"644-653"xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/pages"644-653"xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/title"Structure of dimeric cytochrome c3 from Desulfovibrio gigas at 1.2 A resolution."xsd:string
http://purl.uniprot.org/citations/12657783http://purl.uniprot.org/core/title"Structure of dimeric cytochrome c3 from Desulfovibrio gigas at 1.2 A resolution."xsd:string