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		PDBsum entry 1rof Go to PDB code: Electron transport PDB id 1rof Loading ... Contents Protein chain 60 a.a.* Ligands SF4 * Residue conservation analysis PDB id: 1rof Links PDBe RCSB MMDB JenaLib Proteopedia CATH SCOP PDBSWS ProSAT Name: Electron transport Title: Nmr study of 4fe-4s ferredoxin of thermatoga maritima Structure: Ferredoxin. Chain: a. Engineered: yes. Other_details: 4fe-4s Source: Thermotoga maritima. Organism_taxid: 2336. Gene: potential. Expressed in: escherichia coli. Expression_system_taxid: 562 NMR struc: 10 models Authors: P.Roesch,H.Sticht,G.Wildegger,D.Bentrop,B.Darimont,R.Sterner Key ref: H.Sticht et al. (1996). An NMR-derived model for the solution structure of oxidized Thermotoga maritima 1[Fe4-S4] ferredoxin.Eur J Biochem,237, 726-735.PubMed id: 8647119 Date: 24-Nov-95 Release date: 10-Jun-96 PROCHECK Headers References Protein chain ? P46797 (FER_THEMA) - Ferredoxin from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) Seq:Struc: 60 a.a. 60 a.a. Key: PfamA domain Secondary structure CATH domain Eur J Biochem 237:726-735 (1996) PubMed id: 8647119 An NMR-derived model for the solution structure of oxidized Thermotoga maritima 1[Fe4-S4] ferredoxin. H.Sticht, G.Wildegger, D.Bentrop, B.Darimont, R.Sterner, P.Rösch. ABSTRACT The solution structure of the 60-residue 1[Fe4-S4] ferredoxin from the hyperthermophilic bacterium Thermotoga maritima was determined based on 683 distance and 35 dihedral angle restraints that were obtained from NMR data. In addition, data known from crystallographic studies of ferredoxins was used for modeling of the iron-sulfur cluster and its environment. The protein shows a globular fold very similar to the fold of the related 1[Fe4-S4] ferredoxins from Desulfovibrio gigas and Desulfovibrio africanus, and elements of regular secondary structure similar to those in other ferredoxins were found in the T. maritima protein. In particular, the T. maritima protein displayed a beta-sheet structure made up of strands located at the very NH(2) and COOH termini of the protein, and an internal alpha-helix. The internal beta-sheet observed in the D. gigas and D. africanus ferredoxins could not be confirmed in T. maritima ferredoxin and is thus suggested to be only weakly present or even absent in this protein. This result suggests that thermostability in ferredoxins is not necessarily correlated with the content of stable elements of regular secondary structure. Literature references that cite this PDB file's key reference PubMed id Reference 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 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. 10387062 P.L.Wang, L.Calzolai, K.L.Bren, Q.Teng, F.E.Jenney, P.S.Brereton, J.B.Howard, M.W.Adams, and G.N.La Mar (1999). Secondary structure extensions in Pyrococcus furiosus ferredoxin destabilize the disulfide bond relative to that in other hyperthermostable ferredoxins. Global consequences for the disulfide orientational heterogeneity. Biochemistry,38, 8167-8178. 9283290 C.Liang, and K.Mislow (1997). Topological chirality of iron-sulfur proteins. Biopolymers,42, 411-414. 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 code is shown on the right.