2e0w: Difference between revisions

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New page: left|200px<br /><applet load="2e0w" size="450" color="white" frame="true" align="right" spinBox="true" caption="2e0w, resolution 2.55Å" /> '''T391A precursor muta...
 
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[[Image:2e0w.gif|left|200px]]<br /><applet load="2e0w" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2e0w, resolution 2.55&Aring;" />
'''T391A precursor mutant protein of gamma-Glutamyltranspeptidase from Escherichia coli'''<br />


==Overview==
==T391A precursor mutant protein of gamma-Glutamyltranspeptidase from Escherichia coli==
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.
<StructureSection load='2e0w' size='340' side='right'caption='[[2e0w]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
2E0W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k12 Escherichia coli k12]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2E0W OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</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=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>
==Reference==
</table>
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]
== Function ==
[[Category: Escherichia coli k12]]
[https://www.uniprot.org/uniprot/GGT_ECOLI GGT_ECOLI]  
[[Category: Gamma-glutamyltransferase]]
== Evolutionary Conservation ==
[[Category: Single protein]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Fukuyama, K.]]
Check<jmol>
[[Category: Okada, T.]]
  <jmolCheckbox>
[[Category: Wada, K.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e0/2e0w_consurf.spt"</scriptWhenChecked>
[[Category: gamma-gtp]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
[[Category: maturation]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: ntn hydrolase]]
  </jmolCheckbox>
[[Category: post-translational processing]]
</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].
[[Category: precursor]]
<div style="clear:both"></div>
 
__TOC__
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:53:58 2007''
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Fukuyama K]]
[[Category: Okada T]]
[[Category: Wada K]]

Latest revision as of 08:41, 4 June 2025

T391A precursor mutant protein of gamma-Glutamyltranspeptidase from Escherichia coli

2e0w, resolution 2.55Å

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