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1e77

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(New page: 200px<br /> <applet load="1e77" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e77, resolution 2.69&Aring;" /> '''COMPLEX OF ACTIVE M...)
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[[Image:1e77.gif|left|200px]]<br />
 
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<applet load="1e77" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1e77, resolution 2.69&Aring;" />
 
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'''COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE'''<br />
 
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==Overview==
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==COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE==
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The role of Asp-177 in the His-Asp catalytic dyad of glucose 6-phosphate, dehydrogenase from Leuconostoc mesenteroides has been investigated by a, structural and functional characterization of the D177N mutant enzyme. Its, three-dimensional structure has been determined by X-ray, cryocrystallography in the presence of NAD(+) and in the presence of, glucose 6-phosphate plus NADPH. The structure of a glucose 6-phosphate, complex of a mutant (Q365C) with normal enzyme activity has also been, determined and substrate binding compared. To understand the effect of, Asp-177 on the ionization properties of the catalytic base His-240, the pH, dependence of kinetic parameters has been determined for the D177N mutant, and compared to that of the wild-type enzyme. The structures give details, of ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11106478 (full description)]]
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<StructureSection load='1e77' size='340' side='right'caption='[[1e77]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1e77]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leuconostoc_mesenteroides Leuconostoc mesenteroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E77 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]] 2.69&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1e77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e77 OCA], [https://pdbe.org/1e77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e77 RCSB], [https://www.ebi.ac.uk/pdbsum/1e77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e77 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/G6PD_LEUME G6PD_LEUME]
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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/e7/1e77_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=1e77 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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1E77 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Leuconostoc_mesenteroides Leuconostoc mesenteroides]] with BG6 and CA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E77 OCA]].
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*[[Glucose 6-phosphate dehydrogenase|Glucose 6-phosphate dehydrogenase]]
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__TOC__
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==Reference==
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</StructureSection>
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An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme., Cosgrove MS, Gover S, Naylor CE, Vandeputte-Rutten L, Adams MJ, Levy HR, Biochemistry. 2000 Dec 12;39(49):15002-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11106478 11106478]
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[[Category: Large Structures]]
[[Category: Leuconostoc mesenteroides]]
[[Category: Leuconostoc mesenteroides]]
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[[Category: Single protein]]
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[[Category: Adams MJ]]
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[[Category: Adams, M.J.]]
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[[Category: Gover S]]
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[[Category: Gover, S.]]
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[[Category: Vandeputte-Rutten L]]
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[[Category: Vandeputte-Rutten, L.]]
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[[Category: BG6]]
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[[Category: CA]]
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[[Category: glucose metabolism]]
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[[Category: oxidoreductase (choh(d) - nad(p))]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:14:19 2007''
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Current revision

COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE

PDB ID 1e77

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