View source for 5jh1


==Crystal structure of the apo form of AKR4C7 from maize==
<StructureSection load='5jh1' size='340' side='right'caption='[[5jh1]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jh1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JH1 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]] 1.45&#8491;</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=5jh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jh1 OCA], [https://pdbe.org/5jh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jh1 RCSB], [https://www.ebi.ac.uk/pdbsum/5jh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jh1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A2T1W7_MAIZE A2T1W7_MAIZE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops. However, these AKR4Cs show little to no activity with previously-envisioned sugar substrates. We hypothesized a structural basis for the distinctive cofactor binding and substrate specificity of these plant enzymes. To test this, we solved the crystal structure of a novel AKR4C subfamily member, the AKR4C7 from maize, in the apo form and in complex with NADP(+). The binary complex revealed an intermediate state of cofactor binding that preceded closure of Loop B, and also indicated that conformational changes upon substrate binding are required to induce a catalytically-favorable conformation of the active-site pocket. Comparative structural analyses of homologues (AKR1B1, AKR4C8 and AKR4C9) showed that evolutionary redesign of plant AKR4Cs weakened interactions that stabilize the closed conformation of Loop B. This in turn decreased cofactor affinity and altered configuration of the substrate-binding site. We propose that these structural modifications contribute to impairment of sugar reductase activity in favor of other substrates in the plant AKR4C subgroup, and that catalysis involves a three-step process relevant to other AKRs.

A comparative structural analysis reveals distinctive features of co-factor binding and substrate specificity in plant aldo-keto reductases.,Giuseppe PO, Santos ML, Sousa SM, Koch KE, Yunes JA, Aparicio R, Murakami MT Biochem Biophys Res Commun. 2016 Jun 10;474(4):696-701. doi:, 10.1016/j.bbrc.2016.05.011. Epub 2016 May 3. PMID:27154221<ref>PMID:27154221</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5jh1" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aldo-keto reductase 3D structures|Aldo-keto reductase 3D structures]]
*[[Aldose reductase 3D structures|Aldose reductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Aparicio R]]
[[Category: Giuseppe PO]]
[[Category: Koch KE]]
[[Category: Murakami MT]]
[[Category: Santos ML]]
[[Category: Sousa SM]]
[[Category: Yunes JA]]