1gec

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[[Image:1gec.jpg|left|200px]]
[[Image:1gec.jpg|left|200px]]
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{{Structure
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|PDB= 1gec |SIZE=350|CAPTION= <scene name='initialview01'>1gec</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1gec", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=GLM:1-AMINO-PROPAN-2-ONE'>GLM</scene>, <scene name='pdbligand=PHQ:FORMIC+ACID+BENZYL+ESTER'>PHQ</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycyl_endopeptidase Glycyl endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.25 3.4.22.25] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1gec| PDB=1gec | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gec OCA], [http://www.ebi.ac.uk/pdbsum/1gec PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gec RCSB]</span>
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}}
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'''GLYCYL ENDOPEPTIDASE-COMPLEX WITH BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE COVALENTLY BOUND TO CYSTEINE 25'''
'''GLYCYL ENDOPEPTIDASE-COMPLEX WITH BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE COVALENTLY BOUND TO CYSTEINE 25'''
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[[Category: Ohara, B P.]]
[[Category: Ohara, B P.]]
[[Category: Pearl, L H.]]
[[Category: Pearl, L H.]]
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[[Category: hydrolysis]]
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[[Category: Hydrolysis]]
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[[Category: inhibitor complex]]
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[[Category: Inhibitor complex]]
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[[Category: proteinase]]
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[[Category: Proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:27:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:42:17 2008''
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Revision as of 14:27, 2 May 2008

Image:1gec.jpg

Template:STRUCTURE 1gec

GLYCYL ENDOPEPTIDASE-COMPLEX WITH BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE COVALENTLY BOUND TO CYSTEINE 25


Overview

Glycyl endopeptidase is a cysteine endopeptidase of the papain family, characterized by specificity for cleavage C-terminal to glycyl residues only and by resistance to inhibition by members of the cystatin family of cysteine proteinase inhibitors. Glycyl endopeptidase has been crystallized from high salt with a substrate-like inhibitor covalently bound to the catalytic Cys 25. The structure has been solved by molecular replacement with the structure of papain and refined at 2.1 A to an R factor of 0.196 (Rfree = 0.258) with good geometry. The structure of the S1 substrate binding site of glycyl endopeptidase differs from that of papain by the substitution of glycines at residues 23 and 65 in papain, with glutamic acid and arginine, respectively, in glycyl endopeptidase. The side chains of these residues form a barrier across the binding pocket, effectively excluding substrate residues with large side chains from the S1 subsite. The constriction of this subsite in glycyl endopeptidase explains the unique specificity of this enzyme for cleavage after glycyl residues and is a major component of its resistance to inhibition by cystatins.

About this Structure

1GEC is a Single protein structure of sequence from Carica papaya. Full crystallographic information is available from OCA.

Reference

Crystal structure of glycyl endopeptidase from Carica papaya: a cysteine endopeptidase of unusual substrate specificity., O'Hara BP, Hemmings AM, Buttle DJ, Pearl LH, Biochemistry. 1995 Oct 10;34(40):13190-5. PMID:7548082 Page seeded by OCA on Fri May 2 17:27:56 2008

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