2dbu

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[[Image:2dbu.gif|left|200px]]<br /><applet load="2dbu" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2dbu.gif|left|200px]]
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caption="2dbu, resolution 1.95&Aring;" />
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'''Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli'''<br />
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{{Structure
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|PDB= 2dbu |SIZE=350|CAPTION= <scene name='initialview01'>2dbu</scene>, resolution 1.95&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/Gamma-glutamyltransferase Gamma-glutamyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.2 2.3.2.2]
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|GENE= ggt ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2DBU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Gamma-glutamyltransferase Gamma-glutamyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.2 2.3.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DBU OCA].
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2DBU is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DBU OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16618936 16618936]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16618936 16618936]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Gamma-glutamyltransferase]]
[[Category: Gamma-glutamyltransferase]]
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[[Category: glutathione]]
[[Category: glutathione]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:57:13 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:25:21 2008''

Revision as of 14:25, 20 March 2008


PDB ID 2dbu

Drag the structure with the mouse to rotate
, resolution 1.95Å
Gene: ggt (Escherichia coli)
Activity: Gamma-glutamyltransferase, with EC number 2.3.2.2
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli


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.

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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