1p3c
From Proteopedia
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Glutamyl endopeptidase from Bacillus intermedius
Overview
Extracellular glutamyl endopeptidase from Bacillus intermedius (BIEP) is a, chymotrypsin-like serine protease which cleaves the peptide bond on the, carboxyl side of glutamic acid. Its three-dimensional structure was, determined for C222(1) and C2 crystal forms of BIEP to 1.5 and 1.75 A, resolution, respectively. The topology of BIEP diverges from the most, common chymotrypsin architecture, because one of the domains consists of a, beta-sandwich consisting of two antiparallel beta-sheets and two helices., In the C2 crystals, a 2-methyl-2,4-pentanediol (MPD) molecule was found in, the substrate binding site, mimicking a glutamic acid. This enabled the, identification of the residues involved in the substrate recognition. The, presence of the MPD molecule causes a change in the active site; the, interaction between two catalytic residues (His47 and Ser171) is, disrupted. The N-terminal end of the enzyme is involved in the formation, of the substrate binding pocket. This indicates a direct relation between, zymogen activation and substrate charge compensation.
About this Structure
1P3C is a Single protein structure of sequence from Bacillus intermedius. Full crystallographic information is available from OCA.
Reference
The crystal structure of glutamyl endopeptidase from Bacillus intermedius reveals a structural link between zymogen activation and charge compensation., Meijers R, Blagova EV, Levdikov VM, Rudenskaya GN, Chestukhina GG, Akimkina TV, Kostrov SV, Lamzin VS, Kuranova IP, Biochemistry. 2004 Mar 16;43(10):2784-91. PMID:15005613
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