1NVT

Crystal structure of Shikimate Dehydrogenase (AROE or MJ1084) in complex with NADP+

Summary for 1NVT

• Entry DOI: 10.2210/pdb1nvt/pdb
• Descriptor: Shikimate 5'-dehydrogenase, ZINC ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total)
• Functional Keywords: structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, oxidoreductase
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 2
• Total formula weight: 64272.67

Authors

Padyana, A.K.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2003-02-04, release date: 2003-03-25, Last modification date: 2024-02-14)

Primary citation

Padyana, A.K.,Burley, S.K.
Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution
Structure, 11:1005-1013, 2003

PubMed Abstract: 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.

PubMed: 12906831
DOI: 10.1016/S0969-2126(03)00159-X

Experimental method

X-RAY DIFFRACTION (2.35 Å)