2ctc
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(New page: 200px<br /><applet load="2ctc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ctc, resolution 1.4Å" /> '''THE HIGH RESOLUTION C...)
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Revision as of 07:07, 21 November 2007
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THE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBOXYPEPTIDASE A AND L-PHENYL LACTATE
Overview
The X-ray structures of native carboxypeptidase A and of the, enzyme-inhibitor complex with L-phenyl lactate have been refined at 1.54, and 1.45 A resolution to R factors of 0.151 and 0.161, respectively., Crystals of the complex were isomorphous with the native crystals (space, group P2(1), a = 51.60, b = 60.27, c = 47.25 A, beta = 97.27 degrees )., The high-resolution electron density allowed correction of many side-chain, positions in the classical carboxypeptidase A model. This reflects the, advantages of the high-quality complete synchrotron data collected with an, imaging plate detector. The conformational changes in the active centre of, the enzyme upon binding of the inhibitor are restricted to only two, residues, Tyr248 and Arg145. L-Phenyl lactate is bound in the S1' pocket, and forms hydrogen bonds to Arg145, Glu270 and to the zinc-bound water, molecule. The present structure provides an explanation for the higher, stability of the complexes with the products of esterolysis in comparison, with those of amidolysis. This is consistent with the finding that product, release is rate limiting for esters but not for peptides.
About this Structure
2CTC is a Single protein structure of sequence from Bos taurus with ZN and HFA as ligands. Active as Carboxypeptidase A, with EC number 3.4.17.1 Full crystallographic information is available from OCA.
Reference
High-resolution structure of the complex between carboxypeptidase A and L-phenyl lactate., Teplyakov A, Wilson KS, Orioli P, Mangani S, Acta Crystallogr D Biol Crystallogr. 1993 Nov 1;49(Pt 6):534-40. PMID:15299490
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