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| {{STRUCTURE_1p3e| PDB=1p3e | SCENE= }} | | {{STRUCTURE_1p3e| PDB=1p3e | SCENE= }} |
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| '''Structure of Glu endopeptidase in complex with MPD'''
| | ===Structure of Glu endopeptidase in complex with MPD=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15005613}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15005613 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15005613}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Glu specific]] | | [[Category: Glu specific]] |
| [[Category: Serine protease]] | | [[Category: Serine protease]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:38:00 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:47:40 2008'' |
