1tqh
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(New page: 200px<br /><applet load="1tqh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tqh, resolution 1.63Å" /> '''Covalent Reaction in...)
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Revision as of 01:23, 21 November 2007
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Covalent Reaction intermediate Revealed in Crystal Structure of the Geobacillus stearothermophilus Carboxylesterase Est30
Overview
Est30 is a thermophilic carboxylesterase cloned from Geobacillus, stearothermophilus that showed optimal hydrolysis of esters with short, acyl chains at 70 degrees C. Est30 is a member of a new family of, carboxylesterases with representatives in other Gram-positive bacteria., The crystal structure has been determined at 1.63A resolution using, multiple anomalous dispersion data. The two-domain crystal structure, showed a large domain with a modified alpha/beta hydrolase core including, a seven, rather than an eight-stranded beta sheet, and a smaller cap, domain comprising three alpha helices. The catalytic triad consists of, residues Ser94, Asp193, and His223. A 100Da tetrahedral ligand was, observed to be covalently bound to the side-chain of Ser94. The propyl, acetate ligand represents the first tetrahedral intermediate in the, reaction mechanism. Therefore, this Est30 crystal structure will help, understand the mode of action of all enzymes in the serine hydrolase, superfamily.
About this Structure
1TQH is a Single protein structure of sequence from Geobacillus stearothermophilus with SO4 and 4PA as ligands. Active as Carboxylesterase, with EC number 3.1.1.1 Full crystallographic information is available from OCA.
Reference
Covalent reaction intermediate revealed in crystal structure of the Geobacillus stearothermophilus carboxylesterase Est30., Liu P, Wang YF, Ewis HE, Abdelal AT, Lu CD, Harrison RW, Weber IT, J Mol Biol. 2004 Sep 10;342(2):551-61. PMID:15327954
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