1pl6: Difference between revisions

Latest revision as of 00:22, 21 November 2024

Human SDH/NADH/inhibitor complex

Structural highlights

1pl6 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	572, MSE, NAD, ZN
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Sorbitol dehydrogenase (hSDH) and aldose reductase form the polyol pathway that interconverts glucose and fructose. Redox changes from overproduction of the coenzyme NADH by SDH may play a role in diabetes-induced dysfunction in sensitive tissues, making SDH a therapeutic target for diabetic complications. We have purified and determined the crystal structures of human SDH alone, SDH with NAD(+), and SDH with NADH and an inhibitor that is competitive with fructose. hSDH is a tetramer of identical, catalytically active subunits. In the apo and NAD(+) complex, the catalytic zinc is coordinated by His69, Cys44, Glu70, and a water molecule. The inhibitor coordinates the zinc through an oxygen and a nitrogen atom with the concomitant dissociation of Glu70. The inhibitor forms hydrophobic interactions to NADH and likely sterically occludes substrate binding. The structure of the inhibitor complex provides a framework for developing more potent inhibitors of hSDH.

X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase.,Pauly TA, Ekstrom JL, Beebe DA, Chrunyk B, Cunningham D, Griffor M, Kamath A, Lee SE, Madura R, Mcguire D, Subashi T, Wasilko D, Watts P, Mylari BL, Oates PJ, Adams PD, Rath VL Structure. 2003 Sep;11(9):1071-85. PMID:12962626^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pauly TA, Ekstrom JL, Beebe DA, Chrunyk B, Cunningham D, Griffor M, Kamath A, Lee SE, Madura R, Mcguire D, Subashi T, Wasilko D, Watts P, Mylari BL, Oates PJ, Adams PD, Rath VL. X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase. Structure. 2003 Sep;11(9):1071-85. PMID:12962626

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Pauly TA, Ekstrom JL, Beebe DA, Chrunyk B, Cunningham D, Griffor M, Kamath A, Lee SE, Madura R, Mcguire D, Subashi T, Wasilko D, Watts P, Mylari BL, Oates PJ, Adams PD, Rath VL. X-ray crystallographic and kinetic studies of human sorbitol dehydrogenase. Structure. 2003 Sep;11(9):1071-85. PMID:12962626

[1]

@@ Line 3: / Line 3: @@
 <StructureSection load='1pl6' size='340' side='right'caption='[[1pl6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1pl6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PL6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PL6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1pl6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PL6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=572:4-[2-(HYDROXYMETHYL)PYRIMIDIN-4-YL]-N,N-DIMETHYLPIPERAZINE-1-SULFONAMIDE'>572</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</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&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=572:4-[2-(HYDROXYMETHYL)PYRIMIDIN-4-YL]-N,N-DIMETHYLPIPERAZINE-1-SULFONAMIDE'>572</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pl7|1pl7]], [[1pl8|1pl8]]</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=1pl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pl6 OCA], [https://pdbe.org/1pl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pl6 RCSB], [https://www.ebi.ac.uk/pdbsum/1pl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pl6 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-iditol_2-dehydrogenase L-iditol 2-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.14 1.1.1.14] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pl6 OCA], [http://pdbe.org/1pl6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pl6 RCSB], [http://www.ebi.ac.uk/pdbsum/1pl6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pl6 ProSAT]</span></td></tr>
 </table>
-== Function ==
-[[http://www.uniprot.org/uniprot/DHSO_HUMAN DHSO_HUMAN]] Converts sorbitol to fructose. Part of the polyol pathway that plays an important role in sperm physiology. May play a role in the sperm motility by providing an energetic source for sperm (By similarity).<ref>PMID:16278369</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 17: / Line 13: @@
    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pl/1pl6_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
@@ Line 35: / Line 31: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: L-iditol 2-dehydrogenase]]
 [[Category: Large Structures]]
-[[Category: Adams, P D]]
+[[Category: Adams PD]]
-[[Category: Beebe, D A]]
+[[Category: Beebe DA]]
-[[Category: Chrunyk, B]]
+[[Category: Chrunyk B]]
-[[Category: Cunningham, D]]
+[[Category: Cunningham D]]
-[[Category: Ekstrom, J L]]
+[[Category: Ekstrom JL]]
-[[Category: Griffor, M]]
+[[Category: Griffor M]]
-[[Category: Kamath, A]]
+[[Category: Kamath A]]
-[[Category: Lee, S E]]
+[[Category: Lee SE]]
-[[Category: Madura, R]]
+[[Category: Madura R]]
-[[Category: Mcguire, D]]
+[[Category: Mcguire D]]
-[[Category: Mylari, B L]]
+[[Category: Mylari BL]]
-[[Category: Oates, P J]]
+[[Category: Oates PJ]]
-[[Category: Pauly, T A]]
+[[Category: Pauly TA]]
-[[Category: Rath, V L]]
+[[Category: Rath VL]]
-[[Category: Subashi, T]]
+[[Category: Subashi T]]
-[[Category: Wasilko, D]]
+[[Category: Wasilko D]]
-[[Category: Watts, P]]
+[[Category: Watts P]]
-[[Category: Cp-166]]
-[[Category: Oxidoreductase]]
-[[Category: Sorbitol dehydrogenase]]

1pl6: Difference between revisions

Latest revision as of 00:22, 21 November 2024

Human SDH/NADH/inhibitor complex

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

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