View source for 3qkz


==Crystal structure of mutant His269Arg AKR1B14==
<StructureSection load='3qkz' size='340' side='right'caption='[[3qkz]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qkz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QKZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QKZ 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]] 1.87&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=3qkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qkz OCA], [https://pdbe.org/3qkz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qkz RCSB], [https://www.ebi.ac.uk/pdbsum/3qkz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qkz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALD1_RAT ALD1_RAT] Reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. May play a role in the metabolism of xenobiotic aromatic aldehydes.<ref>PMID:21048316</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rat aldose reductase-like protein (AKR1B14) is an orthologue of mouse vas deferens protein (AKR1B7) and plays roles in the detoxification of reactive aldehydes and synthesis of prostaglandin F(2alpha). Here, the 1.87 A resolution crystal structure of the His269Arg mutant of AKR1B14 complexed with NADPH is described and shows that the negatively charged 2'-phosphate group of the coenzyme forms an ionic interaction with the positively charged guanidinium group of Arg269 that is also observed in the human aldose reductase (AKR1B1) structure. Previous experiments on the site-directed mutagenesis of His269 to Arg, Phe and Met revealed fourfold, sevenfold and 127-fold increases in the K(m) for NADPH, respectively, which are in agreement with the present molecular-modelling and X-ray crystallographic studies. This is the first tertiary structure of a mutant form of this AKR1B7 orthologue to be reported in order to investigate the structure-function relationship of the nonconserved His269 and its role in coenzyme binding.

Structure of the His269Arg mutant of the rat aldose reductase-like protein AKR1B14 complexed with NADPH.,Sundaram K, Endo S, Matsunaga T, Tanaka N, Hara A, El-Kabbani O Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Apr 1;68(Pt 4):400-3. Epub, 2012 Mar 27. PMID:22505406<ref>PMID:22505406</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qkz" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aldo-keto reductase 3D structures|Aldo-keto reductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: El-Kabbani O]]
[[Category: Sundaram K]]