2cwf
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(New page: 200px<br /><applet load="2cwf" size="350" color="white" frame="true" align="right" spinBox="true" caption="2cwf, resolution 1.80Å" /> '''Crystal Structure of...)
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Revision as of 16:49, 29 January 2008
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Crystal Structure of delta1-piperideine-2-carboxylate reductase from Pseudomonas syringae complexed with NADPH
Overview
Delta(1)-Piperideine-2-carboxylate/Delta(1)-pyrroline-2-carboxylate, reductase from Pseudomonas syringae pv. tomato belongs to a novel, sub-class in a large family of NAD(P)H-dependent oxidoreductases distinct, from the conventional MDH/LDH superfamily characterized by the Rossmann, fold. We have determined the structures of the following three forms of, the enzyme: the unliganded form, the complex with NADPH, and the complex, with NADPH and pyrrole-2-carboxylate at 1.55-, 1.8-, and 1.7-A, resolutions, respectively. The enzyme exists as a dimer, and the subunit, consists of three domains; domain I, domain II (NADPH binding domain), and, domain III. The core of the NADPH binding domain consists of a, seven-stranded predominantly antiparallel beta-sheet fold (which we named, SESAS) that is characteristic of the new oxidoreductase family. The enzyme, preference for NADPH over NADH is explained by the cofactor binding site, architecture. A comparison of the overall structures revealed that the, mobile domains I and III change their conformations to produce the, catalytic form. This conformational change plays important roles in, substrate recognition and the catalytic process. The active site structure, of the catalytic form made it possible to identify the catalytic, Asp:Ser:His triad and investigate the catalytic mechanism from a, stereochemical point of view.
About this Structure
2CWF is a Single protein structure of sequence from Pseudomonas syringae pv. tomato with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of Delta1-piperideine-2-carboxylate/Delta1-pyrroline-2-carboxylate reductase belonging to a new family of NAD(P)H-dependent oxidoreductases: conformational change, substrate recognition, and stereochemistry of the reaction., Goto M, Muramatsu H, Mihara H, Kurihara T, Esaki N, Omi R, Miyahara I, Hirotsu K, J Biol Chem. 2005 Dec 9;280(49):40875-84. Epub 2005 Sep 28. PMID:16192274
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