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1m9h

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[[Image:1m9h.jpg|left|200px]]<br /><applet load="1m9h" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1m9h, resolution 2.0&Aring;" />
 
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'''Corynebacterium 2,5-DKGR A and Phe 22 replaced with Tyr (F22Y), Lys 232 replaced with Gly (K232G), Arg 238 replaced with His (R238H)and Ala 272 replaced with Gly (A272G)in presence of NADH cofactor'''<br />
 
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==Overview==
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==Corynebacterium 2,5-DKGR A and Phe 22 replaced with Tyr (F22Y), Lys 232 replaced with Gly (K232G), Arg 238 replaced with His (R238H)and Ala 272 replaced with Gly (A272G)in presence of NADH cofactor==
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Corynebacterium 2,5-Diketo-D-gluconic acid reductase (2,5-DKGR) catalyzes the reduction of 2,5-diketo-D-gluconic acid (2,5-DKG) to 2-Keto-L-gulonic acid (2-KLG). 2-KLG is an immediate precursor to L-ascorbic acid (vitamin C), and 2,5-DKGR is, therefore, an important enzyme in a novel industrial method for the production of vitamin C. 2,5-DKGR, as with most other members of the aldo-keto reductase (AKR) superfamily, exhibits a preference for NADPH compared to NADH as a cofactor in the stereo-specific reduction of substrate. The application of 2,5-DKGR in the industrial production of vitamin C would be greatly enhanced if NADH could be efficiently utilized as a cofactor. A mutant form of 2,5-DKGR has previously been identified that exhibits two orders of magnitude higher activity with NADH in comparison to the wild-type enzyme, while retaining a high level of activity with NADPH. We report here an X-ray crystal structure of the holo form of this mutant in complex with NADH cofactor, as well as thermodynamic stability data. By comparing the results to our previously reported X-ray structure of the holo form of wild-type 2,5-DKGR in complex with NADPH, the structural basis of the differential NAD(P)H selectivity of wild-type and mutant 2,5-DKGR enzymes has been identified.
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<StructureSection load='1m9h' size='340' side='right'caption='[[1m9h]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1m9h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_sp. Corynebacterium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M9H FirstGlance]. <br>
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1M9H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Corynebacterium_sp. Corynebacterium sp.] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9H OCA].
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m9h OCA], [https://pdbe.org/1m9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m9h RCSB], [https://www.ebi.ac.uk/pdbsum/1m9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m9h ProSAT]</span></td></tr>
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Structural alteration of cofactor specificity in Corynebacterium 2,5-diketo-D-gluconic acid reductase., Sanli G, Banta S, Anderson S, Blaber M, Protein Sci. 2004 Feb;13(2):504-12. Epub 2004 Jan 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14718658 14718658]
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</table>
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[[Category: Corynebacterium sp.]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/DKGA_CORSC 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.
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[[Category: Blaber, M.]]
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== Evolutionary Conservation ==
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[[Category: Sanli, G.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: NAD]]
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Check<jmol>
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[[Category: SO4]]
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<jmolCheckbox>
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[[Category: tim-barrel]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m9/1m9h_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:59 2008''
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1m9h ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Corynebacterium sp]]
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[[Category: Large Structures]]
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[[Category: Blaber M]]
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[[Category: Sanli G]]

Current revision

Corynebacterium 2,5-DKGR A and Phe 22 replaced with Tyr (F22Y), Lys 232 replaced with Gly (K232G), Arg 238 replaced with His (R238H)and Ala 272 replaced with Gly (A272G)in presence of NADH cofactor

PDB ID 1m9h

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