2ihu | pdb_00002ihu

Carboxyethylarginine synthase from Streptomyces clavuligerus: putative reaction intermediate complex

spinqualitylabelsall models 2ihu, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ihu is a 4 chain structure with sequence from As 4.1611. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, K, MG, TAR, TP8, TP9 Gene: ceas2 (AS 4.1611) Activity: N(2)-(2-carboxyethyl)arginine synthase, with EC number 2.5.1.66 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum 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 N(2)-(2-Carboxyethyl)arginine synthase (CEAS), an unusual thiamin diphosphate (ThDP)-dependent enzyme, catalyses the committed step in the biosynthesis of the b-lactamase inhibitor clavulanic acid in Streptomyces clavuligerus. Crystal structures of tetrameric CEAS-ThDP in complex with the substrate analogues 5-guanidinovaleric acid (GVA) and tartrate, and a structure reflecting a possible enol(ate)-ThDP reaction intermediate are described. The structures suggest overlapping binding sites for the substrates D-glyceraldehyde-3-phosphate (D-G3P) and L-arginine, and are consistent with the proposed CEAS mechanism in which D-G3P binds at the active site and reacts to form an alpha,beta-unsaturated intermediate,which subsequently undergoes (1,4)-Michael addition with the alpha-amino group of L-arginine. Additional solution studies are presented which probe the amino acid substrate tolerance of CEAS, providing further insight into the L-arginine binding site. These findings may facilitate the engineering of CEAS towards the synthesis of alternative beta-amino acid products. Structural and mechanistic studies on N(2)-(2-carboxyethyl)arginine synthase.,Caines ME, Sorensen JL, Schofield CJ Biochem Biophys Res Commun. 2009 Aug 7;385(4):512-7. Epub 2009 May 27. PMID:19477162 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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