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[[Image:2dbw.png|left|200px]]


{{STRUCTURE_2dbw| PDB=2dbw | SCENE= }}
==Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli Acyl-Enzyme Intermediate==
<StructureSection load='2dbw' size='340' side='right'caption='[[2dbw]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2dbw]] is a 4 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=2DBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DBW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dbw OCA], [https://pdbe.org/2dbw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dbw RCSB], [https://www.ebi.ac.uk/pdbsum/2dbw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dbw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GGT_ECOLI GGT_ECOLI]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/db/2dbw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2dbw ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


===Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli Acyl-Enzyme Intermediate===
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<ref>PMID:16618936</ref>


{{ABSTRACT_PUBMED_16618936}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2dbw" style="background-color:#fffaf0;"></div>
[[2dbw]] is a 4 chain structure with sequence from [http://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=2DBW OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:016618936</ref><references group="xtra"/>
</StructureSection>
[[Category: Escherichia coli k-12]]
[[Category: Escherichia coli K-12]]
[[Category: Gamma-glutamyltransferase]]
[[Category: Large Structures]]
[[Category: Fukuyama, K.]]
[[Category: Fukuyama K]]
[[Category: Okada, T.]]
[[Category: Okada T]]
[[Category: Wada, K.]]
[[Category: Wada K]]
[[Category: Acyl-enzyme intermediate]]
[[Category: Gamma-glutamyltransferase]]
[[Category: Gamma-gtp]]
[[Category: Ggt]]
[[Category: Glutathione]]
[[Category: Transferase]]
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