1p3c: Difference between revisions
New page: left|200px<br /><applet load="1p3c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p3c, resolution 1.50Å" /> '''Glutamyl endopeptida... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1p3c.gif|left|200px]]<br /><applet load="1p3c" size=" | [[Image:1p3c.gif|left|200px]]<br /><applet load="1p3c" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1p3c, resolution 1.50Å" /> | caption="1p3c, resolution 1.50Å" /> | ||
'''Glutamyl endopeptidase from Bacillus intermedius'''<br /> | '''Glutamyl endopeptidase from Bacillus intermedius'''<br /> | ||
==Overview== | ==Overview== | ||
Extracellular glutamyl endopeptidase from Bacillus intermedius (BIEP) is a | 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== | ==About this Structure== | ||
1P3C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_intermedius Bacillus intermedius]. Full crystallographic information is available from [http:// | 1P3C is a [http://en.wikipedia.org/wiki/Single_protein 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=1P3C OCA]. | ||
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Bacillus intermedius]] | [[Category: Bacillus intermedius]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Akimkina, T | [[Category: Akimkina, T V.]] | ||
[[Category: Blagova, E | [[Category: Blagova, E V.]] | ||
[[Category: Chestukhina, G | [[Category: Chestukhina, G G.]] | ||
[[Category: Kostrov, S | [[Category: Kostrov, S V.]] | ||
[[Category: Kuranova, I | [[Category: Kuranova, I P.]] | ||
[[Category: Lamzin, V | [[Category: Lamzin, V S.]] | ||
[[Category: Levdikov, V | [[Category: Levdikov, V M.]] | ||
[[Category: Meijers, R.]] | [[Category: Meijers, R.]] | ||
[[Category: Rudenskaya, G | [[Category: Rudenskaya, G N.]] | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:24:42 2008'' | ||
Revision as of 12:24, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 14:24:42 2008
