2dpg: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2dpg.jpg|left|200px]]<br /><applet load="2dpg" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2dpg, resolution 2.5&Aring;" />
-'''COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+'''<br />
-==Overview==
+==COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+==
-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.
+<StructureSection load='2dpg' size='340' side='right'caption='[[2dpg]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+<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>
+</table>
+== 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>
-==About this Structure==
+==See Also==
-DPG 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/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] Known structural/functional Site: <scene name='pdbsite=NUL:Active Site Mutant, HIS 240 -> ASN. The Base Required To ...'>NUL</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DPG OCA].
+*[[Glucose 6-phosphate dehydrogenase|Glucose 6-phosphate dehydrogenase]]
+__TOC__
-==Reference==
+</StructureSection>
-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]
+[[Category: Large Structures]]
-[[Category: Glucose-6-phosphate 1-dehydrogenase]]
 [[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: NAP]]
-[[Category: choh(d) - nad(p)]]
-[[Category: glucose metabolism]]
-[[Category: nadp/nad]]
-[[Category: oxidoreductase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 19:31:44 2007''