1e8m
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(New page: 200px<br /> <applet load="1e8m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e8m, resolution 1.5Å" /> '''PROLYL OLIGOPEPTIDAS...)
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Revision as of 15:22, 29 October 2007
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PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT, COMPLEXED WITH INHIBITOR
Overview
Structure determination of the inactive S554A variant of prolyl, oligopeptidase complexed with an octapeptide has shown that substrate, binding is restricted to the P4-P2' region. In addition, it has revealed a, hydrogen bond network of potential catalytic importance not detected in, other serine peptidases. This involves a unique intramolecular hydrogen, bond between the P1' amide and P2 carbonyl groups and another between the, P2' amide and Nepsilon2 of the catalytic histidine 680 residue. It is, argued that both hydrogen bonds promote proton transfer from the, imidazolium ion to the leaving group. Another complex formed with the, product-like inhibitor benzyloxycarbonyl-glycyl-proline, indicating that, the carboxyl group of the inhibitor forms a hydrogen bond with the, Nepsilon2 of ... [(full description)]
About this Structure
1E8M is a [Single protein] structure of sequence from [Sus scrofa] with PHQ and GOL as [ligands]. Active as [[1]], with EC number [3.4.21.26]. Full crystallographic information is available from [OCA].
Reference
Structures of prolyl oligopeptidase substrate/inhibitor complexes. Use of inhibitor binding for titration of the catalytic histidine residue., Fulop V, Szeltner Z, Renner V, Polgar L, J Biol Chem. 2001 Jan 12;276(2):1262-6. PMID:11031266
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