2YQ5

Crystal Structure of D-isomer specific 2-hydroxyacid dehydrogenase from Lactobacillus delbrueckii ssp. bulgaricus: NAD complexed form

Summary for 2YQ5

• Entry DOI: 10.2210/pdb2yq5/pdb
• Related: 2YQ4
• Descriptor: D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: LACTOBACILLUS DELBRUECKII SUBSP. BULGARICUS
• Total number of polymer chains: 4
• Total formula weight: 154770.65

Authors

Holton, S.J.,Anandhakrishnan, M.,Geerlof, A.,Wilmanns, M. (deposition date: 2012-11-05, release date: 2012-11-21, Last modification date: 2023-12-20)

Primary citation

Holton, S.J.,Anandhakrishnan, M.,Geerlof, A.,Wilmanns, M.
Structural Characterization of D-Isomer Specific 2-Hydroxyacid Dehydrogenase from Lactobacillus Delbrueckii Ssp. Bulgaricus
J.Struct.Biol., 181:179-, 2013

PubMed Abstract: Hydroxyacid dehydrogenases, responsible for the stereospecific conversion of 2-keto acids to 2-hydroxyacids in lactic acid producing bacteria, have a range of biotechnology applications including antibiotic synthesis, flavor development in dairy products and the production of valuable synthons. The genome of Lactobacillus delbrueckii ssp. bulgaricus, a member of the heterogeneous group of lactic acid bacteria, encodes multiple hydroxyacid dehydrogenases whose structural and functional properties remain poorly characterized. Here, we report the apo and coenzyme NAD⁺ complexed crystal structures of the L. bulgaricusD-isomer specific 2-hydroxyacid dehydrogenase, D2-HDH. Comparison with closely related members of the NAD-dependent dehydrogenase family reveals that whilst the D2-HDH core fold is structurally conserved, the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme.

PubMed: 23110853
DOI: 10.1016/J.JSB.2012.10.009

Experimental method

X-RAY DIFFRACTION (2.75 Å)