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1e77

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

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Retrieved from "http://52.214.119.220/wiki/index.php/1e77"

Categories: Large Structures | Leuconostoc mesenteroides | Adams MJ | Gover S | Vandeputte-Rutten L

@@ Line 1: / Line 1: @@
-[[Image:1e77.gif|left|200px]]
- {{Structure
+==COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE==
-|PDB= 1e77 |SIZE=350|CAPTION= <scene name='initialview01'>1e77</scene>, resolution 2.69&Aring;
+<StructureSection load='1e77' size='340' side='right'caption='[[1e77]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
-|SITE= <scene name='pdbsite=BG6:Bg6+Binding+Site+For+Chain+A'>BG6</scene> and <scene name='pdbsite=CA1:Ca+Binding+Site+For+Chain+A'>CA1</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
+<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>
-|ACTIVITY= [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]
+</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>
-|GENE= G6PD ([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=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=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>
+</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/e7/1e77_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=1e77 ConSurf].
+<div style="clear:both"></div>
-'''COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE'''
+==See Also==
+*[[Glucose 6-phosphate dehydrogenase|Glucose 6-phosphate dehydrogenase]]
+__TOC__
-==Overview==
+</StructureSection>
-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 glucose 6-phosphate binding and show that replacement of the Asp-177 of the catalytic dyad with asparagine does not affect the overall structure of glucose 6-phosphate dehydrogenase. Additionally, the evidence suggests that the productive tautomer of His-240 in the D177N mutant enzyme is stabilized by a hydrogen bond with Asn-177; hence, the mutation does not affect tautomer stabilization. We conclude, therefore, that the absence of a negatively charged aspartate at 177 accounts for the decrease in catalytic activity at pH 7.8. Structural analysis suggests that the pH dependence of the kinetic parameters of D177N glucose 6-phosphate dehydrogenase results from an ionized water molecule replacing the missing negative charge of the mutated Asp-177 at high pH. Glucose 6-phosphate binding orders and orients His-178 in the D177N-glucose 6-phosphate-NADPH ternary complex and appears to be necessary to form this water-binding site.
+[[Category: Large Structures]]
-==About this Structure==
-E77 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=1E77 OCA].
-==Reference==
-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://www.ncbi.nlm.nih.gov/pubmed/11106478 11106478]
-[[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: Vandeputte-Rutten L]]
-[[Category: Vandeputte-Rutten, L.]]
-[[Category: BG6]]
-[[Category: CA]]
-[[Category: glucose metabolism]]
-[[Category: oxidoreductase (choh(d) - nad(p))]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:51:00 2008''

1e77

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

Structural highlights

Function

Evolutionary Conservation

See Also

Contents

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