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2dpg

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(New page: 200px<br /> <applet load="2dpg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dpg, resolution 2.5&Aring;" /> '''COMPLEX OF INACTIVE ...)
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[[Image:2dpg.gif|left|200px]]<br />
 
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<applet load="2dpg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2dpg, resolution 2.5&Aring;" />
 
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'''COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+'''<br />
 
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==Overview==
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==COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+==
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The catalytic mechanism of glucose 6-phosphate dehydrogenase from, Leuconostoc mesenteroides was investigated by replacing three amino acids, His-240, Asp-177, and His 178, with asparagine, using site-directed, mutagenesis. Each of the mutant enzymes was purified to homogeneity and, characterized by substrate binding studies and steady-state kinetic, analyses. The three-dimensional structure of the H240N glucose 6-phosphate, dehydrogenase was determined at 2.5 A resolution. The results support a, mechanism in which His-240 acts as the general base that abstracts the, proton from the C1-hydroxyl group of glucose 6-phosphate, and the, carboxylate group of Asp-177 stabilizes the positive charge that forms on, His-240 in the transition state. The results also confirm the postulated, role of ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9485426 (full description)]]
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<StructureSection load='2dpg' size='340' side='right'caption='[[2dpg]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2dpg]] 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=2DPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DPG 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]] 2.5&#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=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=2dpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dpg OCA], [https://pdbe.org/2dpg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dpg RCSB], [https://www.ebi.ac.uk/pdbsum/2dpg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dpg 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/dp/2dpg_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=2dpg 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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2DPG 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 NAP as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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=2DPG 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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On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase., Cosgrove MS, Naylor C, Paludan S, Adams MJ, Levy HR, Biochemistry. 1998 Mar 3;37(9):2759-67. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9485426 9485426]
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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: Naylor CE]]
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[[Category: Naylor, C.E.]]
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[[Category: Paludin S]]
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[[Category: Paludin, S.]]
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[[Category: NAP]]
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[[Category: choh(d) - nad(p)]]
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[[Category: glucose metabolism]]
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[[Category: nadp/nad]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:34:18 2007''
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Current revision

COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+

PDB ID 2dpg

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