1nvt
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Crystal structure of Shikimate Dehydrogenase (AROE or MJ1084) in complex with NADP+
OverviewOverview
The crystal structure of Methanococcus jannaschii shikimate 5-dehydrogenase (MjSDH) bound to the cofactor nicotinamide adenine dinucleotide phosphate (NADP) has been determined at 2.35 A resolution. Shikimate 5-dehydrogenase (SDH) is responsible for NADP-dependent catalysis of the fourth step in shikimate biosynthesis, which is essential for aromatic amino acid metabolism in bacteria, microbial eukaryotes, and plants. The structure of MjSDH is a compact alpha/beta sandwich with two distinct domains, responsible for binding substrate and the NADP cofactor, respectively. A phylogenetically conserved deep cleft on the protein surface corresponds to the enzyme active site. The structure reveals a topologically new domain fold within the N-terminal segment of the polypeptide chain, which binds substrate and supports dimerization. Insights gained from homology modeling and sequence/structure comparisons suggest that the SDHs represent a unique class of dehydrogenases. The structure provides a framework for further investigation to discover and develop novel inhibitors targeting this essential enzyme.
About this StructureAbout this Structure
1NVT is a Single protein structure of sequence from Methanocaldococcus jannaschii with and as ligands. Active as Shikimate dehydrogenase, with EC number 1.1.1.25 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution., Padyana AK, Burley SK, Structure. 2003 Aug;11(8):1005-13. PMID:12906831
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