1p3e: Difference between revisions
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[[Image:1p3e.gif|left|200px]] | [[Image:1p3e.gif|left|200px]] | ||
'''Structure of Glu endopeptidase in complex with MPD''' | {{Structure | ||
|PDB= 1p3e |SIZE=350|CAPTION= <scene name='initialview01'>1p3e</scene>, resolution 1.72Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Structure of Glu endopeptidase in complex with MPD''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1P3E is a [ | 1P3E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_intermedius Bacillus intermedius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P3E OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15005613 15005613] | ||
[[Category: Bacillus intermedius]] | [[Category: Bacillus intermedius]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:19:17 2008'' | ||
Revision as of 11:19, 20 March 2008
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| 1p3e, resolution 1.72Å | |||||||||||||
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| Ligands: | MPD | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Structure of Glu endopeptidase in complex with MPD
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
1P3E 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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