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1e34
From Proteopedia
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PORCINE PANCREATIC ELASTASE COMPLEXED WITH (3S, 4S)N-PARA-TOLUENESULPHONYL-3-ETHYL-4-(CARBOXYLIC ACID) PYRROLIDIN-2-ONE SOAKED IN PH 9 BUFFER FOR ONE MINUTE
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
1E34 is a [Single protein] structure of sequence from [Sus scrofa] with CA, SO4 and TPX 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 22:00:58 2007
Categories: Single protein | Sus scrofa | Clifton, I.J. | Schofield, C.J. | Wilmouth, R.C. | Wright, P.A. | CA | SO4 | TPX | Hydrolase | Serine protease | Serine proteinase
