1gsh

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(New page: 200px<br /><applet load="1gsh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gsh, resolution 2.0&Aring;" /> '''STRUCTURE OF ESCHERIC...)
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[[Image:1gsh.gif|left|200px]]<br /><applet load="1gsh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gsh, resolution 2.0&Aring;" />
 
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'''STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 7.5'''<br />
 
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==Overview==
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==STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 7.5==
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The crystal structure of Escherichia coli B glutathione synthetase, (GSHase) has been determined at the optimal catalytic condition pH 7.5., The most significant structural difference from the structure at pH 6.0 is, the movement of the central domain towards the N-terminal domain almost as, a rigid body. As a result of this movement, new interdomain and, intersubunit polar interactions are formed which stabilize the dimeric, structure further. The structure of GSHase at optimal pH was compared with, 294 other known protein structures in terms of the spatial arrangements of, secondary structural elements. Three enzymes (D-alanine: D-alanine ligase, succinyl-CoA synthetase and the biotin carboxylase subunit of acetyl-CoA, carboxylase) were found to have structures similar to the ATP-binding site, of GSHase, which extends across two domains. The ATP-binding sites in, these four enzymes are composed of two antiparallel beta-sheets and are, different from the classic mononucleotide-binding fold. Except for these, proteins, no significant structural similarity was detected between GSHase, and the other ATP-binding proteins. A structural motif in the N-terminal, domain of GSHase has been found to be similar to the NAD-binding fold., This structural motif is shared by a number of other proteins that bind, various negatively charged molecules.
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<StructureSection load='1gsh' size='340' side='right'caption='[[1gsh]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gsh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_B Escherichia coli B]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GSH FirstGlance]. <br>
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</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&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gsh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsh OCA], [https://pdbe.org/1gsh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gsh RCSB], [https://www.ebi.ac.uk/pdbsum/1gsh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSHB_ECOLI GSHB_ECOLI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gs/1gsh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1gsh ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1GSH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Glutathione_synthase Glutathione synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.3 6.3.2.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GSH OCA].
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*[[Glutathione synthetase|Glutathione synthetase]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins., Matsuda K, Mizuguchi K, Nishioka T, Kato H, Go N, Oda J, Protein Eng. 1996 Dec;9(12):1083-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9010922 9010922]
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[[Category: Escherichia coli B]]
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Glutathione synthase]]
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[[Category: Kato H]]
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[[Category: Single protein]]
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[[Category: Katsube Y]]
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[[Category: Kato, H.]]
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[[Category: Matsuda K]]
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[[Category: Katsube, Y.]]
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[[Category: Nishioka T]]
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[[Category: Matsuda, K.]]
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[[Category: Oda J]]
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[[Category: Nishioka, T.]]
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[[Category: Yamaguchi H]]
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[[Category: Oda, J.]]
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[[Category: Yamaguchi, H.]]
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[[Category: glutathione biosynthesis]]
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[[Category: glutathione synthase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:16:02 2007''
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Current revision

STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 7.5

PDB ID 1gsh

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