3gk7 | pdb_00003gk7

Crystal structure of 4-hydroxybutyrate CoA-Transferase from Clostridium aminobutyricum

spinqualitylabelsall models 3gk7, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3gk7 is a 2 chain structure with sequence from "clostridium_aminobutyricum"_hardman_and_stadtman "clostridium aminobutyricum" hardman and stadtman. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SPD, TRS Related: 2oas, 3d3u Gene: abfT ("Clostridium aminobutyricum" Hardman and Stadtman) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 4-Hydroxybutyrate CoA-transferases (4-HB-CoAT) takes part in the fermentation of 4-aminobutyrate to ammonia, acetate, and butyrate in anaerobic bacteria such as Clostridium aminobutyricum and Porphyromonas gingivalis or facultative anaerobic bacteria such as Shewanella oneidensis. Site-directed mutagenesis of the highly active enzyme has identified the catalytic glutamate residue as E238. Crystal structure of this enzyme has been determined at a resolution of 1.85 A. The 438-amino acid residue polypeptide chain folds into two topologically similar domains with an open alpha/beta-fold, which is also found in other CoAT family I and family II members. The data indicate that the members of CoAT families I and II are closely related; the latter only lacking the catalytic glutamate residue. A putative co-substrate binding site for the 4-HB-CoAT was identified, in which a 4-hydroxybutyrate molecule has been modeled. This site is also responsible for binding the acetyl group of acetyl-CoA or the succinyl group of succinyl-CoA in succinyl-CoA:3-oxoacid CoA-transferase from mammalian mitochondria. Mutations of relevant active site amino acid residues have been produced and their activities tested to corroborate the proposed structural model for substrate binding. 4-HB-CoAT from C. aminobutyricum represents the only functionally characterized 4-HB-CoAT present in the structural database. Crystal structure of 4-hydroxybutyrate CoA-transferase from Clostridium aminobutyricum.,Macieira S, Zhang J, Velarde M, Buckel W, Messerschmidt A Biol Chem. 2009 Dec;390(12):1251-63. PMID:19804364 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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