2dpg: Difference between revisions

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[[Image:2dpg.jpg|left|200px]]


{{Structure
==COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+==
|PDB= 2dpg |SIZE=350|CAPTION= <scene name='initialview01'>2dpg</scene>, resolution 2.5&Aring;
<StructureSection load='2dpg' size='340' side='right'caption='[[2dpg]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE= <scene name='pdbsite=NUL:Active+Site+Mutant,+HIS+240+-&#62;+ASN.+The+Base+Required+To+...'>NUL</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>
<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>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_1-dehydrogenase Glucose-6-phosphate 1-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </span>
</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>
|GENE= PLMZ/H240N ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1245 Leuconostoc mesenteroides])
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dpg OCA], [http://www.ebi.ac.uk/pdbsum/2dpg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dpg RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/G6PD_LEUME G6PD_LEUME]
== 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/dp/2dpg_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=2dpg ConSurf].
<div style="clear:both"></div>


'''COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+'''
==See Also==
 
*[[Glucose 6-phosphate dehydrogenase|Glucose 6-phosphate dehydrogenase]]
 
__TOC__
==Overview==
</StructureSection>
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 His-178 in binding the phosphate moiety of glucose 6-phosphate.
[[Category: Large Structures]]
 
==About this Structure==
2DPG is a [[Single protein]] structure of sequence from [http://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].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/9485426 9485426]
[[Category: Glucose-6-phosphate 1-dehydrogenase]]
[[Category: Leuconostoc mesenteroides]]
[[Category: Leuconostoc mesenteroides]]
[[Category: Single protein]]
[[Category: Adams MJ]]
[[Category: Adams, M J.]]
[[Category: Gover S]]
[[Category: Gover, S.]]
[[Category: Naylor CE]]
[[Category: Naylor, C E.]]
[[Category: Paludin S]]
[[Category: Paludin, S.]]
[[Category: choh(d) - nad(p)]]
[[Category: glucose metabolism]]
[[Category: nadp/nad]]
[[Category: oxidoreductase]]
 
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Retrieved from "https://proteopedia.org/2dpg"