2kkd | pdb_00002kkd

NMR Structure of Ni Substitued Desulfovibrio vulgaris Rubredoxin

spinqualitylabelsall models 2kkd, 15 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kkd is a 1 chain structure with sequence from Desvh. This structure supersedes the now removed PDB entry 2qkz. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NI Related: 8rxn, 2ql0 Gene: rub, DVU_3184 (DESVH) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RUBR_DESVH] Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule. Electron acceptor for cytoplasmic lactate dehydrogenase. 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 Ni(II) and Zn(II) derivatives of Desulfovibrio vulgaris rubredoxin (DvRd) have been studied by NMR spectroscopy to probe the structure at the metal centre. The betaCH(2) proton pairs from the cysteines that bind the Ni(II) atom have been identified using 1D nuclear Overhauser enhancement (NOE) difference spectra and sequence specifically assigned via NOE correlations to neighbouring protons and by comparison with the published X-ray crystal structure of a Ni(II) derivative of Clostridium pasteurianum rubredoxin. The solution structures of DvRd(Zn) and DvRd(Ni) have been determined and the paramagnetic form refined using pseudocontact shifts. The determination of the magnetic susceptibility anisotropy tensor allowed the contact and pseudocontact contributions to the observed chemical shifts to be obtained. Analysis of the pseudocontact and contact chemical shifts of the cysteine Hbeta protons and backbone protons close to the metal centre allowed conclusions to be drawn as to the geometry and hydrogen-bonding pattern at the metal binding site. The importance of NH-S hydrogen bonds at the metal centre for the delocalization of electron spin density is confirmed for rubredoxins and can be extrapolated to metal centres in Cu proteins: amicyanin, plastocyanin, stellacyanin, azurin and pseudoazurin. An NMR structural study of nickel-substituted rubredoxin.,Goodfellow BJ, Duarte IC, Macedo AL, Volkman BF, Nunes SG, Moura I, Markley JL, Moura JJ J Biol Inorg Chem. 2009 Dec 8. PMID:19997764 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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