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		PDBsum entry 1gx7 Go to PDB code: Oxidoreductase PDB id 1gx7 Loading ... Contents Protein chains 371 a.a.* 88 a.a.* 107 a.a.* Ligands SF4 ×3 PDT CYN ×2 CMO ×2 HEC ×4 Metals FE2×2 * Residue conservation analysis Theoretical model PDB id: 1gx7 Links PDBe RCSB MMDB JenaLib Proteopedia CATH SCOP PDBSWS CSA PROCOGNATE ProSAT Name: Oxidoreductase Title: Best model of the electron transfer complex between cytochrome c3 and [fe]-hydrogenase Structure: Periplasmic [fe] hydrogenase large subunit. Chain: a. Periplasmic [fe] hydrogenase small subunit. Chain: d. Cytochrome c3. Chain: e Source: Desulfovibrio vulgaris. Organism_taxid: 882. Strain: hildenborough. Strain: hildenborough NMR struc: 1 models Authors: L.Elantak,X.Morelli,O.Bornet,C.Hatchikian,M.Czjzek,A.Dolla, F.Guerlesquin Key ref: L.ElAntak et al. (2003). The cytochrome c3-[Fe]-hydrogenase electron-transfer complex: structural model by NMR restrained docking.FEBS Lett,548, 1-4.PubMed id: 12885397 DOI: 10.1016/S0014-5793(03)00718-X Date: 28-Mar-02 Release date: 31-Jul-03 PROCHECK Headers References Protein chain ? P07598 (PHFL_DESVH) - Periplasmic [Fe] hydrogenase large subunit from Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) Seq:Struc: 421 a.a. 371 a.a. Protein chain ? P07603 (PHFS_DESVH) - Periplasmic [Fe] hydrogenase small subunit from Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) Seq:Struc: 123 a.a. 88 a.a. Protein chain ? P00131 (CYC3_DESVH) - Cytochrome c3 from Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) Seq:Struc: 129 a.a. 107 a.a. Key: PfamA domain Secondary structure Enzyme reactions Enzyme class: Chains A, D: E.C.1.12.7.2 - ferredoxin hydrogenase. [IntEnz] [ExPASy] [KEGG] [BRENDA] Reaction: H2 + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H+ + 2 reduced [2Fe-2S]- [ferredoxin] Cofactor: Iron-sulfur; Ni(2+) Iron-sulfur Ni(2+) Molecule diagrams generated from .mol files obtained from theKEGG ftp site Key reference DOI no: 10.1016/S0014-5793(03)00718-X FEBS Lett 548:1-4 (2003) PubMed id: 12885397 The cytochrome c3-[Fe]-hydrogenase electron-transfer complex: structural model by NMR restrained docking. L.ElAntak, X.Morelli, O.Bornet, C.Hatchikian, M.Czjzek, A.Dolla, F.Guerlesquin. ABSTRACT Cytochrome c(3) (M(r) 13000) is a low redox potential cytochrome specific of the anaerobic metabolism in sulfate-reducing bacteria. This tetrahemic cytochrome is an intermediate between the [Fe]-hydrogenase and the cytochrome Hmc in Desulfovibrio vulgaris Hildenborough strain. The present work describes the structural model of the cytochrome c(3)-[Fe]-hydrogenase complex obtained by nuclear magnetic resonance restrained docking. This model connects the distal cluster of the [Fe]-hydrogenase to heme 4 of the cytochrome, the same heme found in the interaction with cytochrome Hmc. This result gives evidence that cytochrome c(3) is an electron shuttle between the periplasmic hydrogenase and the Hmc membrane-bound complex. Selected figure(s) Figure 3. Fig. 3. A: Ribbon representation of the best representative structure of the [Fe]-hydrogenase–cytochrome c[3] complex. The [Fe]-hydrogenase is the left polypeptide chain, the large subunit is colored in beige; the small subunit is colored in yellow and the ferredoxin-like domain in blue, the iron clusters are in green. Cytochrome c[3] is the right polypeptide chain colored in blue, the heme groups are in red. B: Zoom-in view of the interface region, highlighting the residues involved in interatomic contacts within the cytochrome c[3]–[Fe]-hydrogenase complex. Heme 4 and cytochrome c[3] residues are labeled in red, distal [4Fe–4S] cluster and residues of [Fe]-hydrogenase are labeled in green. Figure 4. Fig. 4. A possible mechanism for ALAD in which both A- and P-side substrates form Schiff bases with the enzyme. The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS Lett (2003,548, 1-4) copyright 2003. Figures were selected by an automated process. Literature references that cite this PDB file's key reference PubMed id Reference 19233927 X.Li, Q.Luo, N.Q.Wofford, K.L.Keller, M.J.McInerney, J.D.Wall, and L.R.Krumholz (2009). A molybdopterin oxidoreductase is involved in H2 oxidation in Desulfovibrio desulfuricans G20. J Bacteriol,191, 2675-2682. 16964504 R.O.Louro (2007). Proton thrusters: overview of the structural and functional features of soluble tetrahaem cytochromes c3. J Biol Inorg Chem,12, 1. 16836469 M.Ihara, H.Nakamoto, T.Kamachi, I.Okura, and M.Maeda (2006). Photoinduced hydrogen production by direct electron transfer from photosystem I cross-linked with cytochrome c3 to [NiFe]-hydrogenase. Photochem Photobiol,82, 1677-1685. 16341896 R.E.Di Paolo, P.M.Pereira, I.Gomes, F.M.Valente, I.A.Pereira, and R.Franco (2006). Resonance Raman fingerprinting of multiheme cytochromes from the cytochrome c3 family. J Biol Inorg Chem,11, 217-224. 15853810 C.A.Salgueiro, L.Morgado, B.Fonseca, P.Lamosa, T.Catarino, D.L.Turner, and R.O.Louro (2005). Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein. FEBS J,272, 2251-2260. 15764652 L.Rivas, C.M.Soares, A.M.Baptista, J.Simaan, R.E.Di Paolo, D.H.Murgida, and P.Hildebrandt (2005). Electric-field-induced redox potential shifts of tetraheme cytochromes c3 immobilized on self-assembled monolayers: surface-enhanced resonance Raman spectroscopy and simulation studies. Biophys J,88, 4188-4199. 14594815 M.Fournier, Z.Dermoun, M.C.Durand, and A.Dolla (2004). A new function of the Desulfovibrio vulgaris Hildenborough [Fe] hydrogenase in the protection against oxidative stress. J Biol Chem,279, 1787-1793. 15386621 M.Prudêncio, and M.Ubbink (2004). Transient complexes of redox proteins: structural and dynamic details from NMR studies. J Mol Recognit,17, 524-539. The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.