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| [[Image:2e0w.gif|left|200px]]
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| {{Structure
| | ==T391A precursor mutant protein of gamma-Glutamyltranspeptidase from Escherichia coli== |
| |PDB= 2e0w |SIZE=350|CAPTION= <scene name='initialview01'>2e0w</scene>, resolution 2.55Å
| | <StructureSection load='2e0w' size='340' side='right'caption='[[2e0w]], [[Resolution|resolution]] 2.55Å' scene=''> |
| |SITE=
| | == Structural highlights == |
| |LIGAND=
| | <table><tr><td colspan='2'>[[2e0w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E0W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E0W FirstGlance]. <br> |
| |ACTIVITY= <span class='plainlinks'>[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] </span>
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55Å</td></tr> |
| |GENE= ggt ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K12])
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e0w OCA], [https://pdbe.org/2e0w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e0w RCSB], [https://www.ebi.ac.uk/pdbsum/2e0w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e0w ProSAT]</span></td></tr> |
| |DOMAIN=
| | </table> |
| |RELATEDENTRY=[[2dbu|2DBU]]
| | == Function == |
| |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e0w OCA], [http://www.ebi.ac.uk/pdbsum/2e0w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e0w RCSB]</span>
| | [https://www.uniprot.org/uniprot/GGT_ECOLI GGT_ECOLI] |
| }}
| | == Evolutionary Conservation == |
| | | [[Image:Consurf_key_small.gif|200px|right]] |
| '''T391A precursor mutant protein of gamma-Glutamyltranspeptidase from Escherichia coli'''
| | Check<jmol> |
| | | <jmolCheckbox> |
| | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e0/2e0w_consurf.spt"</scriptWhenChecked> |
| ==Overview== | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| 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.
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | | </jmolCheckbox> |
| ==About this Structure== | | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2e0w ConSurf]. |
| 2E0W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k12 Escherichia coli k12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E0W OCA].
| | <div style="clear:both"></div> |
| | | __TOC__ |
| ==Reference== | | </StructureSection> |
| 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 K-12]] |
| [[Category: Escherichia coli k12]] | | [[Category: Large Structures]] |
| [[Category: Gamma-glutamyltransferase]]
| | [[Category: Fukuyama K]] |
| [[Category: Single protein]] | | [[Category: Okada T]] |
| [[Category: Fukuyama, K.]] | | [[Category: Wada K]] |
| [[Category: Okada, T.]] | |
| [[Category: Wada, K.]] | |
| [[Category: gamma-gtp]]
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| [[Category: maturation]]
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| [[Category: ntn hydrolase]]
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| [[Category: post-translational processing]]
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| [[Category: precursor]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:42:04 2008''
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