1ynq

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[[Image:1ynq.gif|left|200px]]
 
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==aldo-keto reductase AKR11C1 from Bacillus halodurans (holo form)==
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The line below this paragraph, containing "STRUCTURE_1ynq", creates the "Structure Box" on the page.
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<StructureSection load='1ynq' size='340' side='right'caption='[[1ynq]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1ynq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalobacillus_halodurans_C-125 Alkalihalobacillus halodurans C-125]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YNQ FirstGlance]. <br>
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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]] 1.3&#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=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1ynq| PDB=1ynq | SCENE= }}
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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=1ynq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ynq OCA], [https://pdbe.org/1ynq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ynq RCSB], [https://www.ebi.ac.uk/pdbsum/1ynq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ynq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9KE47_HALH5 Q9KE47_HALH5]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yn/1ynq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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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=1ynq ConSurf].
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<div style="clear:both"></div>
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'''aldo-keto reductase AKR11C1 from Bacillus halodurans (holo form)'''
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==See Also==
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*[[Aldo-keto reductase 3D structures|Aldo-keto reductase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Aldo-keto reductase AKR11C1 from Bacillus halodurans, a new member of aldo-keto reductase (AKR) family 11, has been characterized structurally and biochemically. The structures of the apo and NADPH bound form of AKR11C1 have been solved to 1.25 A and 1.3 A resolution, respectively. AKR11C1 possesses a novel non-aromatic stacking interaction of an arginine residue with the cofactor, which may favor release of the oxidized cofactor. Our biochemical studies have revealed an NADPH-dependent activity of AKR11C1 with 4-hydroxy-2,3-trans-nonenal (HNE). HNE is a cytotoxic lipid peroxidation product, and detoxification in alkaliphilic bacteria, such as B.halodurans, plays a crucial role in survival. AKR11C1 could thus be part of the detoxification system, which ensures the well being of the microorganism. The very poor activity of AKR11C1 on standard, small substrates such as benzaldehyde or DL-glyeraldehyde is consistent with the observed, very open active site lacking a binding pocket for these substrates. In contrast, modeling of HNE with its aldehyde function suitably positioned in the active site suggests that its elongated hydrophobic tail occupies a groove defined by hydrophobic side-chains. Multiple sequence alignment of AKR11C1 with the highly homologous iolS and YqkF proteins shows a high level of conservation in this putative substrate-binding site. We suggest that AKR11C1 is the first structurally characterized member of a new class of AKRs with specificity for substrates with long aliphatic tails.
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[[Category: Alkalihalobacillus halodurans C-125]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Kostrewa D]]
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1YNQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_halodurans Bacillus halodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YNQ OCA].
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[[Category: Li XD]]
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[[Category: Marquardt T]]
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==Reference==
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[[Category: Winkler FK]]
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High-resolution crystal structure of AKR11C1 from Bacillus halodurans: an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase., Marquardt T, Kostrewa D, Balakrishnan R, Gasperina A, Kambach C, Podjarny A, Winkler FK, Balendiran GK, Li XD, J Mol Biol. 2005 Nov 25;354(2):304-16. Epub 2005 Oct 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16242712 16242712]
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[[Category: Bacillus halodurans]]
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[[Category: Single protein]]
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[[Category: Kostrewa, D.]]
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[[Category: Li, X D.]]
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[[Category: Marquardt, T.]]
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[[Category: Winkler, F K.]]
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[[Category: Akr11c1]]
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[[Category: Aldo-keto reductase]]
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[[Category: Bacillus haloduran]]
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[[Category: Nadph]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:33:20 2008''
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Current revision

aldo-keto reductase AKR11C1 from Bacillus halodurans (holo form)

PDB ID 1ynq

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