1p3c: Difference between revisions

[[Image:1p3c.gif|left|200px]]<br /><applet load="1p3c" size="350" color="white" frame="true" align="right" spinBox="true"  

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.

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].  

[[Category: Akimkina, T V.]]

[[Category: Blagova, E V.]]

[[Category: Chestukhina, G G.]]

[[Category: Kostrov, S V.]]

[[Category: Kuranova, I P.]]

[[Category: Lamzin, V S.]]

[[Category: Levdikov, V M.]]

[[Category: Rudenskaya, G N.]]

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