1p3c: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1p3c]] is a 1 chain structure with 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=1P3C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P3C FirstGlance]. <br> | <table><tr><td colspan='2'>[[1p3c]] is a 1 chain structure with 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=1P3C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P3C FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p3e|1p3e]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p3e|1p3e]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p3c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p3c RCSB], [http://www.ebi.ac.uk/pdbsum/1p3c PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p3c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p3c RCSB], [http://www.ebi.ac.uk/pdbsum/1p3c PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus intermedius]] | [[Category: Bacillus intermedius]] | ||
[[Category: Akimkina, T V | [[Category: Akimkina, T V]] | ||
[[Category: Blagova, E V | [[Category: Blagova, E V]] | ||
[[Category: Chestukhina, G G | [[Category: Chestukhina, G G]] | ||
[[Category: Kostrov, S V | [[Category: Kostrov, S V]] | ||
[[Category: Kuranova, I P | [[Category: Kuranova, I P]] | ||
[[Category: Lamzin, V S | [[Category: Lamzin, V S]] | ||
[[Category: Levdikov, V M | [[Category: Levdikov, V M]] | ||
[[Category: Meijers, R | [[Category: Meijers, R]] | ||
[[Category: Rudenskaya, G N | [[Category: Rudenskaya, G N]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Serine protease]] | [[Category: Serine protease]] | ||
Revision as of 11:21, 6 January 2015
Glutamyl endopeptidase from Bacillus intermediusGlutamyl endopeptidase from Bacillus intermedius
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedExtracellular 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 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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