View source for 5hws


==Crystal structure of ketopantoate reductase from Thermococcus kodakarensis complexed with NADP+==
<StructureSection load='5hws' size='340' side='right'caption='[[5hws]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hws]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HWS 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]] 2.3&#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=5hws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hws OCA], [https://pdbe.org/5hws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hws RCSB], [https://www.ebi.ac.uk/pdbsum/5hws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hws ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PANE_THEKO PANE_THEKO] Catalyzes the NAD(P)H-dependent reduction of ketopantoate into pantoic acid. Prefers NADH rather than NADPH as the electron donor.<ref>PMID:23941541</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Coenzyme A (CoA) plays pivotal roles in a variety of metabolic pathways in all organisms. The biosynthetic pathway of CoA is strictly regulated by feedback inhibition. In the hyperthermophilic archaeon Thermococcus kodakarensis, ketopantoate reductase (KPR), which catalyzes the NAD(P)H-dependent reduction of 2-oxopantoate, is a target of feedback inhibition by CoA. The crystal structure of KPR from T. kodakarensis (Tk-KPR) complexed with CoA and 2-oxopantoate has previously been reported. The structure provided an explanation for the competitive inhibition mechanism. Here, further biochemical analyses of Tk-KPR and the crystal structure of Tk-KPR in complex with NADP(+) are reported. A mutational analysis implies that the residues in the binding pocket cooperatively contribute to the recognition of CoA. The structure reveals the same dimer architecture as the Tk-KPR-CoA-2-oxopantoate complex. Moreover, the positions of the residues involved in the dimer interaction are not changed by the binding of CoA and 2-oxopantoate, suggesting individual conformational changes of Tk-KPR monomers.

Crystal structure of ketopantoate reductase from Thermococcus kodakarensis complexed with NADP(.).,Aikawa Y, Nishitani Y, Tomita H, Atomi H, Miki K Acta Crystallogr F Struct Biol Commun. 2016 May 1;72(Pt 5):369-75. doi:, 10.1107/S2053230X16005033. Epub 2016 Apr 22. PMID:27139828<ref>PMID:27139828</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5hws" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermococcus kodakarensis KOD1]]
[[Category: Aikawa Y]]
[[Category: Miki K]]
[[Category: Nishitani Y]]