1p3e: Difference between revisions

Revision as of 15:24, 21 February 2008

Structure of Glu endopeptidase in complex with MPD

OverviewOverview

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 StructureAbout this Structure

1P3E is a Single protein structure of sequence from Bacillus intermedius with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-[[Image:1p3e.gif|left|200px]]<br /><applet load="1p3e" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1p3e.gif|left|200px]]<br /><applet load="1p3e" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1p3e, resolution 1.72&Aring;" />
 '''Structure of Glu endopeptidase in complex with MPD'''<br />
 ==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.
+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==
-P3E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_intermedius Bacillus intermedius] with MPD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P3E OCA].
+P3E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_intermedius Bacillus intermedius] with <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P3E OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Bacillus intermedius]]
 [[Category: Single protein]]
-[[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: Rudenskaya, G.N.]]
+[[Category: Rudenskaya, G N.]]
 [[Category: MPD]]
 [[Category: glu specific]]
 [[Category: serine protease]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:54:55 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:24:42 2008''