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1WMB

Crystal structure of NAD dependent D-3-hydroxybutylate dehydrogenase

Summary for 1WMB
Entry DOI10.2210/pdb1wmb/pdb
DescriptorD(-)-3-hydroxybutyrate dehydrogenase, MAGNESIUM ION, CACODYLATE ION, ... (4 entities in total)
Functional Keywordsnad, nadh, short chain dehydrogenase, oxidoreductase
Biological sourcePseudomonas fragi
Total number of polymer chains2
Total formula weight53747.42
Authors
Ito, K.,Nakajima, Y.,Ichihara, E.,Ogawa, K.,Yoshimoto, T. (deposition date: 2004-07-06, release date: 2005-09-06, Last modification date: 2024-03-13)
Primary citationIto, K.,Nakajima, Y.,Ichihara, E.,Ogawa, K.,Katayama, N.,Nakashima, K.,Yoshimoto, T.
d-3-Hydroxybutyrate Dehydrogenase from Pseudomonas fragi: Molecular Cloning of the Enzyme Gene and Crystal Structure of the Enzyme
J.Mol.Biol., 355:722-733, 2006
Cited by
PubMed Abstract: The gene coding for d-3-hydroxybutyrate dehydrogenase (HBDH) was cloned from Pseudomonas fragi. The nucleotide sequence contained a 780 bp open reading frame encoding a 260 amino acid residue protein. The recombinant enzyme was efficiently expressed in Escherichia coli cells harboring pHBDH11 and was purified to homogeneity as judged by SDS-PAGE. The enzyme showed a strict stereospecificity to the D-enantiomer (3R-configuration) of 3-hydroxybutyrate as a substrate. Crystals of the ligand-free HBDH and of the enzyme-NAD+ complex were obtained using the hanging-drop, vapor-diffusion method. The crystal structure of the HBDH was solved by the multiwavelength anomalous diffraction method using the SeMet-substituted enzyme and was refined to 2.0 A resolution. The overall structure of P.fragi HBDH, including the catalytic tetrad of Asn114, Ser142, Tyr155, and Lys159, shows obvious relationships with other members of the short-chain dehydrogenase/reductase (SDR) family. A cacodylate anion was observed in both the ligand-free enzyme and the enzyme-NAD+ complex, and was located near the catalytic tetrad. It was shown that the cacodylate inhibited the NAD+-dependent D-3-hydroxybutyrate dehydrogenation competitively, with a Ki value of 5.6 mM. From the interactions between cacodylate and the enzyme, it is predicted that substrate specificity is achieved through the recognition of the 3-methyl and carboxyl groups of the substrate.
PubMed: 16325199
DOI: 10.1016/j.jmb.2005.10.072
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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