1gec
From Proteopedia
(New page: 200px<br /><applet load="1gec" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gec, resolution 2.1Å" /> '''GLYCYL ENDOPEPTIDASE-...) |
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| - | [[Image:1gec.jpg|left|200px]]<br /><applet load="1gec" size=" | + | [[Image:1gec.jpg|left|200px]]<br /><applet load="1gec" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gec, resolution 2.1Å" /> | caption="1gec, resolution 2.1Å" /> | ||
'''GLYCYL ENDOPEPTIDASE-COMPLEX WITH BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE COVALENTLY BOUND TO CYSTEINE 25'''<br /> | '''GLYCYL ENDOPEPTIDASE-COMPLEX WITH BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE COVALENTLY BOUND TO CYSTEINE 25'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Glycyl endopeptidase is a cysteine endopeptidase of the papain family, characterized by specificity for cleavage C-terminal to glycyl residues | + | 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== | ==About this Structure== | ||
| - | 1GEC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Carica_papaya Carica papaya]. Active as [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] Full crystallographic information is available from [http:// | + | 1GEC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Carica_papaya Carica papaya]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GEC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Glycyl endopeptidase]] | [[Category: Glycyl endopeptidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Buttle, D | + | [[Category: Buttle, D J.]] |
| - | [[Category: Hemmings, A | + | [[Category: Hemmings, A M.]] |
| - | [[Category: Ohara, B | + | [[Category: Ohara, B P.]] |
| - | [[Category: Pearl, L | + | [[Category: Pearl, L H.]] |
[[Category: hydrolysis]] | [[Category: hydrolysis]] | ||
[[Category: inhibitor complex]] | [[Category: inhibitor complex]] | ||
[[Category: proteinase]] | [[Category: proteinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:49:07 2008'' |
Revision as of 10:49, 21 February 2008
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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. Active as Glycyl endopeptidase, with EC number 3.4.22.25 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
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