1p3c: Difference between revisions

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[[Image:1p3c.gif|left|200px]]
{{Seed}}
[[Image:1p3c.png|left|200px]]


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{{STRUCTURE_1p3c|  PDB=1p3c  |  SCENE=  }}  
{{STRUCTURE_1p3c|  PDB=1p3c  |  SCENE=  }}  


'''Glutamyl endopeptidase from Bacillus intermedius'''
===Glutamyl endopeptidase from Bacillus intermedius===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15005613}}


==About this Structure==
==About this Structure==
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[[Category: Rudenskaya, G N.]]
[[Category: Rudenskaya, G N.]]
[[Category: Serine protease]]
[[Category: Serine protease]]
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Revision as of 02:07, 29 July 2008

File:1p3c.png

Template:STRUCTURE 1p3c

Glutamyl endopeptidase from Bacillus intermedius

Template:ABSTRACT PUBMED 15005613

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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