5JE8

The crystal structure of Bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD

Summary for 5JE8

• Entry DOI: 10.2210/pdb5je8/pdb
• Descriptor: 3-hydroxyisobutyrate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (5 entities in total)
• Functional Keywords: dehydrogenase, oxidoreductase
• Biological source: Bacillus cereus ATCC 14579
• Total number of polymer chains: 4
• Total formula weight: 134188.97

Authors

Park, S.C.,Yoon, S.I. (deposition date: 2016-04-18, release date: 2016-05-11, Last modification date: 2023-11-08)

Primary citation

Park, S.C.,Kim, P.H.,Lee, G.S.,Kang, S.G.,Ko, H.J.,Yoon, S.I.
Structural and biochemical characterization of the Bacillus cereus 3-hydroxyisobutyrate dehydrogenase
Biochem.Biophys.Res.Commun., 474:522-527, 2016

PubMed Abstract: The 3-hydroxyisobutyrate dehydrogenase (HIBADH) family catalyzes the NAD(+)- or NADP(+)-dependent oxidation of various β-hydroxyacid substrates into their cognate semialdehydes for diverse metabolic pathways. Because HIBADH group members exhibit different substrate specificities, the substrate-recognition mode of each enzyme should be individually characterized. In the current study, we report the biochemical and structural analysis of a HIBADH group enzyme from Bacillus cereus (bcHIBADH). bcHIBADH mediates a dehydrogenation reaction on S-3-hydroxyisobutyrate substrate with high catalytic efficiency in an NAD(+)-dependent manner; it also oxidizes l-serine and 3-hydroxypropionate with lower activity. bcHIBADH consists of two domains and is further assembled into a functional dimer rather than a tetramer that has been commonly observed in other prokaryotic HIBADH group members. In the bcHIBADH structure, the interdomain cleft forms a putative active site and simultaneously accommodates both an NAD(+) cofactor and a substrate mimic. Our structure-based comparative analysis highlights structural motifs that are important in the cofactor and substrate recognition of the HIBADH group.

PubMed: 27120461
DOI: 10.1016/j.bbrc.2016.04.126

Experimental method

X-RAY DIFFRACTION (2.1 Å)