We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2dg5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
 +
{{Seed}}
[[Image:2dg5.gif|left|200px]]
[[Image:2dg5.gif|left|200px]]
Line 9: Line 10:
{{STRUCTURE_2dg5| PDB=2dg5 | SCENE= }}
{{STRUCTURE_2dg5| PDB=2dg5 | SCENE= }}
-
'''Crystal Structure of Gamma-glutamyl transpeptidase from Escherichia coli in complex with hydrolyzed Glutathione'''
+
===Crystal Structure of Gamma-glutamyl transpeptidase from Escherichia coli in complex with hydrolyzed Glutathione===
-
==Overview==
+
<!--
-
Gamma-glutamyltranspeptidase (GGT) is a heterodimic enzyme that is generated from the precursor protein through posttranslational processing and catalyzes the hydrolysis of gamma-glutamyl bonds in gamma-glutamyl compounds such as glutathione and/or the transfer of the gamma-glutamyl group to other amino acids and peptides. We have determined the crystal structure of GGT from Escherichia coli K-12 at 1.95 A resolution. GGT has a stacked alphabetabetaalpha fold comprising the large and small subunits, similar to the folds seen in members of the N-terminal nucleophile hydrolase superfamily. The active site Thr-391, the N-terminal residue of the small subunit, is located in the groove, from which the pocket for gamma-glutamyl moiety binding follows. We have further determined the structure of the gamma-glutamyl-enzyme intermediate trapped by flash cooling the GGT crystal soaked in glutathione solution and the structure of GGT in complex with l-glutamate. These structures revealed how the gamma-glutamyl moiety and l-glutamate are recognized by the enzyme. A water molecule was seen on the carbonyl carbon of the gamma-glutamyl-Thr-391 Ogamma bond in the intermediate that is to be hydrolyzed. Notably the residues essential for GGT activity (Arg-114, Asp-433, Ser-462, and Ser-463 in E. coli GGT) shown by site-directed mutagenesis of human GGT are all involved in the binding of the gamma-glutamyl moiety. The structure of E. coli GGT presented here, together with sequence alignment of GGTs, may be applicable to interpret the biochemical and genetic data of other GGTs.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16618936}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16618936 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16618936}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Ggt]]
[[Category: Ggt]]
[[Category: Glutathione]]
[[Category: Glutathione]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:21:34 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:23:53 2008''

Revision as of 15:23, 28 July 2008

Image:2dg5.gif

Template:STRUCTURE 2dg5

Crystal Structure of Gamma-glutamyl transpeptidase from Escherichia coli in complex with hydrolyzed Glutathione

Template:ABSTRACT PUBMED 16618936

About this Structure

2DG5 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate., Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K, Proc Natl Acad Sci U S A. 2006 Apr 25;103(17):6471-6. Epub 2006 Apr 17. PMID:16618936

Page seeded by OCA on Mon Jul 28 18:23:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2dg5"
Personal tools