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1e36

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[[Category: serine proteinase]]
[[Category: serine proteinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:26:18 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:04:39 2007''

Revision as of 12:59, 30 October 2007


1e36, resolution 1.70Å

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PORCINE PANCREATIC ELASTASE COMPLEXED WITH (3S, 4S)N-PARA-NITROBENZENESULPHONYL-3-ETHYL-4-(CARBOXYLIC ACID)PYRROLIDIN-2-ONE

Overview

beta-Lactams inhibit a range of enzymes via acylation of nucleophilic, serine residues. Certain gamma-lactam analogues of monocyclic beta-lactams, have also been shown to be reversible inhibitors of porcine pancreatic, elastase (PPE), forming acyl-enzyme complexes that are stable with respect, to hydrolysis. Crystallographic analysis at pH 5 of an acyl-enzyme complex, formed with PPE and one of these inhibitors revealed the ester carbonyl, located in the oxyanion hole in a similar conformation to that observed in, the structure of a complex formed between a heptapeptide, (beta-casomorphin-7) and PPE. Only weak electron density was observed for, the His-57 side chain in its 'native' conformation. Instead, the His-57, side chain predominantly adopted a conformation rotated approx. 90 ... [(full description)]

About this Structure

1E36 is a [Single protein] structure of sequence from [Sus scrofa] with CA, SO4 and TPY as [ligands]. Active as [Pancreatic elastase], with EC number [3.4.21.36]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].

Reference

'pH-jump' crystallographic analyses of gamma-lactam-porcine pancreatic elastase complexes., Wright PA, Wilmouth RC, Clifton IJ, Schofield CJ, Biochem J. 2000 Oct 15;351 Pt 2:335-40. PMID:11023818

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