1gec: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:1gec.jpg|left|200px]]
{{Seed}}
[[Image:1gec.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gec|  PDB=1gec  |  SCENE=  }}  
{{STRUCTURE_1gec|  PDB=1gec  |  SCENE=  }}  


'''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===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_7548082}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7548082 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_7548082}}


==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Inhibitor complex]]
[[Category: Inhibitor complex]]
[[Category: Proteinase]]
[[Category: Proteinase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:27:56 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:09:51 2008''

Revision as of 02:09, 1 July 2008

File:1gec.png

Template:STRUCTURE 1gec

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

Template:ABSTRACT PUBMED 7548082

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 Tue Jul 1 05:09:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1gec&oldid=601821"