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| | {{STRUCTURE_2dbu| PDB=2dbu | SCENE= }} | | {{STRUCTURE_2dbu| PDB=2dbu | SCENE= }} |
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| - | '''Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli'''
| + | ===Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli=== |
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| - | ==Overview==
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| - | 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. |
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| | + | {{ABSTRACT_PUBMED_16618936}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Ggt]] | | [[Category: Ggt]] |
| | [[Category: Glutathione]] | | [[Category: Glutathione]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 00:07:55 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:18:37 2008'' |
Revision as of 14:18, 27 July 2008
Template:STRUCTURE 2dbu
Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli
Template:ABSTRACT PUBMED 16618936
About this Structure
2DBU 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
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