5HWS
Crystal structure of ketopantoate reductase from Thermococcus kodakarensis complexed with NADP+
Summary for 5HWS
| Entry DOI | 10.2210/pdb5hws/pdb |
| Descriptor | 2-dehydropantoate 2-reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | oxidoreductase, nadp, rossmann type fold |
| Biological source | Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) |
| Total number of polymer chains | 4 |
| Total formula weight | 139200.70 |
| Authors | Aikawa, Y.,Nishitani, Y.,Miki, K. (deposition date: 2016-01-29, release date: 2016-05-18, Last modification date: 2023-11-08) |
| Primary citation | Aikawa, Y.,Nishitani, Y.,Tomita, H.,Atomi, H.,Miki, K. Crystal structure of ketopantoate reductase from Thermococcus kodakarensis complexed with NADP+ Acta Crystallogr.,Sect.F, 72:369-375, 2016 Cited by PubMed Abstract: 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. PubMed: 27139828DOI: 10.1107/S2053230X16005033 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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