2xec | pdb_00002xec

Nocardia farcinica maleate cis-trans isomerase bound to TRIS

spinqualitylabelsall models 2xec, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2xec is a 4 chain structure with sequence from Nocardia farcinica IFM 10152. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: CA, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MAIA_NOCFA Catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Shows a strict specificity for maleate, with no activity detected toward structurally related substrates including citraconate, mesaconate, dimethylmaleate, and maleamide. 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 Maleate isomerase (MI), a member of the Asp/Glu racemase superfamily, catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Mutational studies, in conjunction with the structure of the C194A mutant of Nocardia farcinica MI cocrystallized with maleate, have revealed an unprecedented mode of catalysis for the superfamily in which the isomerization reaction is initiated by nucleophilic attack of cysteine at the double bond, yielding a covalent succinylcysteine-like intermediate. A Covalent Succinylcysteine-like Intermediate in the Enzyme-Catalyzed Transformation of Maleate to Fumarate by Maleate Isomerase.,Fisch F, Fleites CM, Delenne M, Baudendistel N, Hauer B, Turkenburg JP, Hart S, Bruce NC, Grogan G J Am Chem Soc. 2010 Aug 2. PMID:20677745 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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