1gvk
From Proteopedia
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PORCINE PANCREATIC ELASTASE ACYL ENZYME AT 0.95 A RESOLUTION
Overview
Kinetic analyses led to the discovery that N-acetylated tripeptides with, polar residues at P3 are inhibitors of porcine pancreatic elastase (PPE), that form unusually stable acyl-enzyme complexes. Peptides terminating in, a C-terminal carboxylate were more potent than those terminating in a, C-terminal amide, suggesting recognition by the oxy-anion hole is, important in binding. X-ray diffraction data were recorded to 0.95-A, resolution for an acyl-enzyme complex formed between PPE and, N-acetyl-Asn-Pro-Ile-CO2H at approximately pH 5. The accuracy of the, crystallographic coordinates allows structural issues concerning the, mechanism of serine proteases to be addressed. Significantly, the ester, bond of the acyl-enzyme showed a high level of planarity, suggesting, geometric strain of the ... [(full description)]
About this Structure
1GVK is a [Protein complex] structure of sequences from [Sus scrofa] with CA, SO4 and ACE as [ligands]. Active as [[1]], with EC number [3.4.21.36]. Full crystallographic information is available from [OCA].
Reference
X-ray structure of a serine protease acyl-enzyme complex at 0.95-A resolution., Katona G, Wilmouth RC, Wright PA, Berglund GI, Hajdu J, Neutze R, Schofield CJ, J Biol Chem. 2002 Jun 14;277(24):21962-70. Epub 2002 Mar 14. PMID:11896054
Page seeded by OCA on Mon Oct 29 20:38:39 2007
