Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 81, Issue 11, Pages 2045-2051Publisher
WILEY-BLACKWELL
DOI: 10.1002/prot.24334
Keywords
family VIII carboxylesterases; EstU1; crystal structure of EstU1; crystal structure of the EstU1; cephalothin complex; -lactamase activity
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Funding
- National Research Foundation of Korea [2012005978]
- CAP through KRCF
- CAP through KIST
- CAP through KIOST
- Marine and Extreme Genome Research Center program
- Development of Biohydrogen Production Technology Using Hyperthermophilic Archaea program of MLTM
- KIOST in-house NSC program
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EstU1 is a unique family VIII carboxylesterase that displays hydrolytic activity toward the amide bond of clinically used -lactam antibiotics as well as the ester bond of p-nitrophenyl esters. EstU1 assumes a -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 -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 -lactam antibiotics. This result explains the weak -lactamase activity of EstU1 compared with class C -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. Proteins 2013; 81:2045-2051. (c) 2013 Wiley Periodicals, Inc.
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