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1e38

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(New page: 200px<br /> <applet load="1e38" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e38, resolution 1.70&Aring;" /> '''PORCINE PANCREATIC ...)
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Revision as of 19:56, 29 October 2007

Image:1e38.gif

1e38, 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 SOAKED IN PH 9 BUFFER FOR 2 MINUTES

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

1E38 is a [Single protein] structure of sequence from [Sus scrofa] with CA, SO4 and TPY as [ligands]. Active as [[1]], with EC number [3.4.21.36]. 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

Page seeded by OCA on Mon Oct 29 22:01:25 2007

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