1h9a: 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:1h9a.gif|left|200px]]<br />
-<applet load="1h9a" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1h9a, resolution 2.16&Aring;" />
-'''COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM L. MESENTEROIDES WITH COENZYME NADP'''<br />
-==Overview==
+==COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM L. MESENTEROIDES WITH COENZYME NADP==
-The reduced coenzymes NADH and NADPH only differ by one phosphate, but in, the cell NADH provides reducing power for catabolism while NADPH is, utilized in biosynthetic pathways. Enzymes almost invariably discriminate, between the coenzymes, but glucose 6-phosphate dehydrogenase (G6PD) from, Leuconostoc mesenteroides is rare in being functionally dual specific. In, order to elucidate the coenzyme selectivity, the structures of NADP(+)-, and NAD(+)-complexed L. mesenteroides G6PD have been determined including, data to 2.2 and 2.5 A resolution, respectively, and compared with, unliganded G6PD crystallized in the same space groups. Coenzyme binding is, also compared with that in a ternary complex of a mutant in which Asp177, in the active site has been mutated to asparagine. There are no ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11320304 (full description)]]
+<StructureSection load='1h9a' size='340' side='right'caption='[[1h9a]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1h9a]] 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=1H9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H9A 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]] 2.16&#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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1h9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h9a OCA], [https://pdbe.org/1h9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h9a RCSB], [https://www.ebi.ac.uk/pdbsum/1h9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h9a 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/h9/1h9a_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=1h9a ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The reduced coenzymes NADH and NADPH only differ by one phosphate, but in the cell NADH provides reducing power for catabolism while NADPH is utilized in biosynthetic pathways. Enzymes almost invariably discriminate between the coenzymes, but glucose 6-phosphate dehydrogenase (G6PD) from Leuconostoc mesenteroides is rare in being functionally dual specific. In order to elucidate the coenzyme selectivity, the structures of NADP(+)- and NAD(+)-complexed L. mesenteroides G6PD have been determined including data to 2.2 and 2.5 A resolution, respectively, and compared with unliganded G6PD crystallized in the same space groups. Coenzyme binding is also compared with that in a ternary complex of a mutant in which Asp177 in the active site has been mutated to asparagine. There are no gross structural differences between the complexes. In both binary complexes, the enzyme interdomain hinge angle has opened. NADP(+) binds to the furthest open form; of the residues within the coenzyme domain, only Arg46 moves, interacting with the 2'-phosphate and adenine. NAD(+) is less well defined in the binding site; smaller hinge opening is seen but larger local changes: Arg46 is displaced, Thr14 bonds the 3'-hydroxyl and Gln47 bonds the 2'-hydroxyl. In the ternary complex, the hinge angle has closed; only the adenine nucleotide is ordered in the binding site. Arg46 again provides most binding interactions.
-==About this Structure==
+NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes.,Naylor CE, Gover S, Basak AK, Cosgrove MS, Levy HR, Adams MJ Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):635-48. Epub 2001, Apr 24. PMID:11320304<ref>PMID:11320304</ref>
-H9A 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 SO4 and NAP as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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]]. Structure known Active Sites: NDP and SUL. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H9A OCA]].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes., Naylor CE, Gover S, Basak AK, Cosgrove MS, Levy HR, Adams MJ, Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):635-48. Epub 2001, Apr 24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11320304 11320304]
+</div>
-[[Category: Glucose-6-phosphate 1-dehydrogenase]]
+<div class="pdbe-citations 1h9a" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Glucose 6-phosphate dehydrogenase|Glucose 6-phosphate dehydrogenase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[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: NAP]]
-[[Category: SO4]]
-[[Category: glucose metabolism]]
-[[Category: oxidoreductase (choh(d) - nad(p))]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:32:41 2007''