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[[Image:1a80.gif|left|200px]]<br /><applet load="1a80" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1a80, resolution 2.1&Aring;" />
'''NATIVE 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE A FROM CORYNBACTERIUM SP. COMPLEXED WITH NADPH'''<br />


==Overview==
==Native 2,5-DIKETO-D-GLUCONIC acid reductase a from CORYNBACTERIUM SP. complexed with nadph==
The three-dimensional structure of Corynebacterium 2, 5-diketo-D-gluconic, acid reductase A (2,5-DKGR A; EC 1.1.1.-), in complex with cofactor NADPH, has been solved by using x-ray crystallographic data to 2.1-A resolution., This enzyme catalyzes stereospecific reduction of 2,5-diketo-D-gluconate, (2,5-DKG) to 2-keto-L-gulonate. Thus the three-dimensional structure has, now been solved for a prokaryotic example of the aldo-keto reductase, superfamily. The details of the binding of the NADPH cofactor help to, explain why 2,5-DKGR exhibits lower binding affinity for cofactor than the, related human aldose reductase does. Furthermore, changes in the local, loop structure near the cofactor suggest that 2,5-DKGR will not exhibit, the biphasic cofactor binding characteristics observed in aldose, reductase. Although the crystal structure does not include substrate, the, two ordered water molecules present within the substrate-binding pocket, are postulated to provide positional landmarks for the substrate 5-keto, and 4-hydroxyl groups. The structural basis for several previously, described active-site mutants of 2,5-DKGR A is also proposed. Recent, research efforts have described a novel approach to the synthesis of, L-ascorbate (vitamin C) by using a genetically engineered microorganism, that is capable of synthesizing 2,5-DKG from glucose and subsequently is, transformed with the gene for 2,5-DKGR. These modifications create a, microorganism capable of direct production of 2-keto-L-gulonate from, D-glucose, and the gulonate can subsequently be converted into vitamin C., In economic terms, vitamin C is the single most important specialty, chemical manufactured in the world. Understanding the structural, determinants of specificity, catalysis, and stability for 2,5-DKGR A is of, substantial commercial interest.
<StructureSection load='1a80' size='340' side='right'caption='[[1a80]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1a80]] 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=1A80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A80 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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=1a80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a80 OCA], [https://pdbe.org/1a80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a80 RCSB], [https://www.ebi.ac.uk/pdbsum/1a80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a80 ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== 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/a8/1a80_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1a80 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of Corynebacterium 2, 5-diketo-D-gluconic acid reductase A (2,5-DKGR A; EC 1.1.1.-), in complex with cofactor NADPH, has been solved by using x-ray crystallographic data to 2.1-A resolution. This enzyme catalyzes stereospecific reduction of 2,5-diketo-D-gluconate (2,5-DKG) to 2-keto-L-gulonate. Thus the three-dimensional structure has now been solved for a prokaryotic example of the aldo-keto reductase superfamily. The details of the binding of the NADPH cofactor help to explain why 2,5-DKGR exhibits lower binding affinity for cofactor than the related human aldose reductase does. Furthermore, changes in the local loop structure near the cofactor suggest that 2,5-DKGR will not exhibit the biphasic cofactor binding characteristics observed in aldose reductase. Although the crystal structure does not include substrate, the two ordered water molecules present within the substrate-binding pocket are postulated to provide positional landmarks for the substrate 5-keto and 4-hydroxyl groups. The structural basis for several previously described active-site mutants of 2,5-DKGR A is also proposed. Recent research efforts have described a novel approach to the synthesis of L-ascorbate (vitamin C) by using a genetically engineered microorganism that is capable of synthesizing 2,5-DKG from glucose and subsequently is transformed with the gene for 2,5-DKGR. These modifications create a microorganism capable of direct production of 2-keto-L-gulonate from D-glucose, and the gulonate can subsequently be converted into vitamin C. In economic terms, vitamin C is the single most important specialty chemical manufactured in the world. Understanding the structural determinants of specificity, catalysis, and stability for 2,5-DKGR A is of substantial commercial interest.


==About this Structure==
Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-A resolution.,Khurana S, Powers DB, Anderson S, Blaber M Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6768-73. PMID:9618487<ref>PMID:9618487</ref>
1A80 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 NAP as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=CIC:The Residue Line The Active Site Of Enzyme'>CIC</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A80 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of 2,5-diketo-D-gluconic acid reductase A complexed with NADPH at 2.1-A resolution., Khurana S, Powers DB, Anderson S, Blaber M, Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6768-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9618487 9618487]
</div>
[[Category: Corynebacterium sp.]]
<div class="pdbe-citations 1a80" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Anderson, S.]]
<references/>
[[Category: Blaber, M.]]
__TOC__
[[Category: Khurana, S.]]
</StructureSection>
[[Category: Powers, D.B.]]
[[Category: Corynebacterium sp]]
[[Category: NAP]]
[[Category: Large Structures]]
[[Category: 2]]
[[Category: Anderson S]]
[[Category: 5-diketo-d-gluconic acid]]
[[Category: Blaber M]]
[[Category: alpha8/beta8 barrel]]
[[Category: Khurana S]]
[[Category: commercial vitamin c synthesis]]
[[Category: Powers DB]]
[[Category: oxidoreductase]]
 
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