2cjn | pdb_00002cjn

STRUCTURE OF FERREDOXIN, NMR, MINIMIZED AVERAGE STRUCTURE

spinqualitylabelsall models 2cjn, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2cjn is a 1 chain structure with sequence from Synechococcus elongatus. This structure supersedes the now removed PDB entry 1cjn. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2cjo Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [FER_SYNEL] Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The three-dimensional structure of ferredoxin, purified from the thermophilic cyanobacterium Synechococcus elongatus, was determined in aqueous solution by two-dimensional proton nuclear magnetic resonance. In addition to the 946 distance constraints from nuclear Overhauser effect connectivities, we added 241 distance constraints derived from the crystal structure of Spirulina platensis ferredoxin to the 19 residues close to the [2Fe-2S] iron-sulfur center, where crosspeaks disappeared due to paramagnetic effects. The atomic root-mean-square difference of the ten converged structures from the mean structure was 0.61(+/-0.12) A for backbone atoms (N, C(alpha), C'). The main-chain structure was almost the same as the crystal structures of other mesophile ferredoxins, but comparison of the side-chain structures revealed an extension of the hydrophobic core, a unique hydrophobic patch on the surface of the large beta-sheet, and two unique charge networks in this thermostable ferredoxin structure, some of which might contribute to thermostability. Solution structure of ferredoxin from the thermophilic cyanobacterium Synechococcus elongatus and its thermostability.,Hatanaka H, Tanimura R, Katoh S, Inagaki F J Mol Biol. 1997 May 23;268(5):922-33. PMID:9180381 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferredoxin 3D structures

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