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spacer spacer PDBsum entry 1blu Go to PDB code: protein ligands links Electron transport PDB id 1blu Loading ... JSmol PyMol Contents Protein chain 80 a.a.* Ligands SF4 ×2 Waters ×85 * Residue conservation analysis PDB id: 1blu Links PDBe RCSB MMDB JenaLib Proteopedia CATH SCOP PDBSWS PDBePISA ProSAT Name: Electron transport Title: Structure of the 2[4fe-4s] ferredoxin from chromatium vinosum Structure: Ferredoxin. Chain: a Source: Allochromatium vinosum. Organism_taxid: 1049 Resolution: 2.10Å R-factor: 0.192 Authors: Z.Dauter,K.S.Wilson,L.C.Sieker,J.M.Moulis Key ref: J.M.Moulis et al. (1996). Crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum: evolutionary and mechanistic inferences for [3/4Fe-4S] ferredoxins.Protein Sci,5, 1765-1775.PubMed id: 8880900 DOI: 10.1002/pro.5560050902 Date: 16-Apr-96 Release date: 08-Nov-96 PROCHECK Go to PROCHECK summary Headers References Protein chain Pfam ArchSchema ? P00208 (FER_ALLVD) - Ferredoxin from Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) Seq:Struc: 83 a.a. 80 a.a. Key: PfamA domain Secondary structure CATH domain DOI no: 10.1002/pro.5560050902 Protein Sci 5:1765-1775 (1996) PubMed id: 8880900 Crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum: evolutionary and mechanistic inferences for [3/4Fe-4S] ferredoxins. J.M.Moulis, L.C.Sieker, K.S.Wilson, Z.Dauter. ABSTRACT The crystal structure of the 2[4Fe-4S] ferredoxin from Chromatium vinosum has been solved by molecular replacement using data recorded with synchrotron radiation. The crystals were hexagonal prisms that showed a strong tendency to develop into long tubes. The hexagonal prisms diffracted to 2.1 A resolution at best, and a structural model for C. vinosum ferredoxin has been built with a final R of 19.2%. The N-terminal domain coordinates the two [4Fe-4S] clusters in a fold that is almost identical to that of other known ferredoxins. However, the structure has two unique features. One is a six-residue insertion between two ligands of one cluster forming a two-turn external loop; this short loop changes the conformation of the Cys 40 ligand compared to other ferredoxins and hampers the building of one NH...S H-bond to one of the inorganic sulfurs. The other remarkable structural element is a 3.5-turn alpha-helix at the C-terminus that covers one side of the same cluster and is linked to the cluster-binding domain by a six-residue external chain segment. The charge distribution is highly asymmetric over the molecule. The structure of C. vinosum ferredoxin strongly suggests divergent evolution for bacterial [3/4Fe-4S] ferredoxins from a common ancestral cluster-binding core. The unexpected slow intramolecular electron transfer rate between the clusters in C. vinosum ferredoxin, compared to other similar proteins, may be attributed to the unusual electronic properties of one of the clusters arising from localized changes in its vicinity rather than to a global structural rearrangement. Literature references that cite this PDB file's key reference PubMed id Reference 20635418 B.S.Perrin, and T.Ichiye (2010). Fold versus sequence effects on the driving force for protein-mediated electron transfer. Proteins,78, 2798-2808. 21029451 S.Elsen, G.Efthymiou, P.Peteinatos, G.Diallinas, P.Kyritsis, and J.M.Moulis (2010). A bacteria-specific 2[4Fe-4S] ferredoxin is essential in Pseudomonas aeruginosa. BMC Microbiol,10, 271. 19290553 E.Saridakis, P.Giastas, G.Efthymiou, V.Thoma, J.M.Moulis, P.Kyritsis, and I.M.Mavridis (2009). Insight into the protein and solvent contributions to the reduction potentials of [4Fe-4S]2+/+ clusters: crystal structures of the Allochromatium vinosum ferredoxin variants C57A and V13G and the homologous Escherichia coli ferredoxin. J Biol Inorg Chem,14, 783-799. PDB codes: 2zvs 3eun 3exy 19820092 Y.L.Chiang, Y.C.Hsieh, J.Y.Fang, E.H.Liu, Y.C.Huang, P.Chuankhayan, J.Jeyakanthan, M.Y.Liu, S.I.Chan, and C.J.Chen (2009). Crystal structure of Adenylylsulfate reductase from Desulfovibrio gigas suggests a potential self-regulation mechanism involving the C terminus of the beta-subunit. J Bacteriol,191, 7597-7608. PDB code: 3gyx 17992543 J.Meyer (2008). Iron-sulfur protein folds, iron-sulfur chemistry, and evolution. J Biol Inorg Chem,13, 157-170. 17457690 M.Heinnickel, and J.H.Golbeck (2007). Heliobacterial photosynthesis. Photosynth Res,92, 35-53. 16596388 P.Giastas, N.Pinotsis, G.Efthymiou, M.Wilmanns, P.Kyritsis, J.M.Moulis, and I.M.Mavridis (2006). The structure of the 2[4Fe-4S] ferredoxin from Pseudomonas aeruginosa at 1.32-A resolution: comparison with other high-resolution structures of ferredoxins and contributing structural features to reduction potential values. J Biol Inorg Chem,11, 445-458. PDB code: 2fgo 14747735 M.Unciuleac, M.Boll, E.Warkentin, and U.Ermler (2004). Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin. Acta Crystallogr D Biol Crystallogr,60, 388-391. PDB code: 1rgv 12220497 H.Raaijmakers, S.Macieira, J.M.Dias, S.Teixeira, S.Bursakov, R.Huber, J.J.Moura, I.Moura, and M.J.Romão (2002). Gene sequence and the 1.8 A crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas. Structure,10, 1261-1272. PDB code: 1h0h 11463610 B.W.Beck, Q.Xie, and T.Ichiye (2001). Sequence determination of reduction potentials by cysteinyl hydrogen bonds and peptide pipoles in [4Fe-4S] ferredoxins. Biophys J,81, 601-613. 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. Where a reference describes a PDB structure, the PDB codes are shown on the right. spacer spacer