1hw6: Difference between revisions
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<StructureSection load='1hw6' size='340' side='right' caption='[[1hw6]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1hw6' size='340' side='right' caption='[[1hw6]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hw6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1hw6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Corsp Corsp]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HW6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HW6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a80|1a80]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a80|1a80]]</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=1hw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hw6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hw6 RCSB], [http://www.ebi.ac.uk/pdbsum/1hw6 PDBsum]</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=1hw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hw6 OCA], [http://pdbe.org/1hw6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hw6 RCSB], [http://www.ebi.ac.uk/pdbsum/1hw6 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1hw6" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Corsp]] | ||
[[Category: Blaber, M]] | [[Category: Blaber, M]] | ||
[[Category: Sanli, G]] | [[Category: Sanli, G]] | ||
Revision as of 08:24, 10 September 2015
CRYSTAL STRUCTURE OF APO-2,5-DIKETO-D-GLUCONATE REDUCTASECRYSTAL STRUCTURE OF APO-2,5-DIKETO-D-GLUCONATE REDUCTASE
Structural highlights
Function[DKGA_CORSC] Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates. 25DKGR-A exhibits a greater selectivity for the substrate and higher thermal stability than 25DKGR-B. 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 PubMedA 1.9 A resolution X-ray structure of the apo-form of Corynebacterium 2,5-diketo-d-gluconic acid reductase A (2,5-DKGR A), a member of the aldo-keto reductase superfamily, has been determined by molecular replacement using the NADPH-bound form of the same enzyme as the search model. 2,5-DKGR A catalyzes the NADPH-dependent stereo-specific reduction of 2,5-diketo-d-gluconate (2,5-DKG) to 2-keto-l-gulonate, a precursor in the industrial production of vitamin C. An atomic-resolution structure for the apo-form of the enzyme, in conjunction with our previously reported high-resolution X-ray structure for the holo-enzyme and holo/substrate model, allows a comparative analysis of structural changes that accompany cofactor binding. The results show that regions of the active site undergo coordinated conformational changes of up to 8 A. These conformational changes result in the organization and structural rearrangement of residues associated with substrate binding and catalysis. Thus, NADPH functions not only to provide a hydride ion for catalytic reduction, but is also a critical structural component for formation of a catalytically competent form of DKGR A. Structural assembly of the active site in an aldo-keto reductase by NADPH cofactor.,Sanli G, Blaber M J Mol Biol. 2001 Jun 22;309(5):1209-18. PMID:11399090[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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