4ivi | pdb_00004ivi

Crystal structure of a family VIII carboxylesterase.

spinqualitylabelsall models 4ivi, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ivi is a 1 chain structure with sequence from Uncultured bacterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 NonStd Res: MSE Related: 4ivk Activity: Carboxylesterase, with EC number 3.1.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed EstU1 is a unique family VIII carboxylesterase that displays hydrolytic activity towards the amide bond of clinically used beta-lactam antibiotics as well as the ester bond of p-nitrophenyl esters. EstU1 assumes a beta-lactamase-like modular architecture and contains the residues Ser100, Lys103, and Tyr218, which correspond to the three catalytic residues (Ser64, Lys67, and Tyr150, respectively) of class C beta-lactamases. The structure of the EstU1/cephalothin complex demonstrates that the active site of EstU1 is not ideally tailored to perform an efficient deacylation reaction during the hydrolysis of beta-lactam antibiotics. This result explains the weak beta-lactamase activity of EstU1 compared with class C beta-lactamases. Finally, structural and sequential comparison of EstU1 with other family VIII carboxylesterases elucidates an operative molecular strategy used by family VIII carboxylesterases to extend their substrate spectrum. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc. Structural basis for the beta-lactamase activity of EstU1, a family VIII carboxylesterase.,Cha SS, Jun An Y, Jeong CS, Kim MK, Jeon JH, Lee CM, Lee HS, Gyun Kang S, Lee JH Proteins. 2013 Jun 5. doi: 10.1002/prot.24334. PMID:23737193 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Carboxylesterase

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