Binary Structure of the Two-Domain ( 3R)-Hydroxyacyl-CoA Dehydrogenase from Rat Peroxisomal Multifunctional Enzyme Type 2 at 2.38 Å Resolution

The crystal structure of (3 R)-hydroxyacyl-CoA dehydrogenase of rat peroxisomal multifunctional enzyme type 2 (MFE-2) was solved at 2.38 Å resolution. The catalytic entity reveals an α/β short chain alcohol dehydrogenase/reductase (SDR) fold and the conformation of the bound nicotinamide adenine din...

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Bibliographic Details
Published in:Structure (London) 2003, Vol.11 (1), p.87-97
Main Authors: Haapalainen, Antti M., Koski, M.Kristian, Qin, Yong-Mei, Hiltunen, J.Kalervo, Glumoff, Tuomo
Format: Article
Language:English
Subjects:
17β-HSD
3-Hydroxyacyl CoA Dehydrogenases - chemistry
3-Hydroxyacyl CoA Dehydrogenases - genetics
3-Hydroxyacyl CoA Dehydrogenases - metabolism
Amino Acid Sequence
Animals
Crystallography, X-Ray
Dimerization
Enoyl-CoA Hydratase - chemistry
Enoyl-CoA Hydratase - genetics
Humans
MFE-2
Models, Molecular
Molecular Sequence Data
Multienzyme Complexes - chemistry
Multienzyme Complexes - genetics
NAD(H)
peroxisome
Peroxisomes - enzymology
Protein Structure, Quaternary
Rats
Rats, Wistar
SDR
Sequence Alignment
β oxidation
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Summary:The crystal structure of (3 R)-hydroxyacyl-CoA dehydrogenase of rat peroxisomal multifunctional enzyme type 2 (MFE-2) was solved at 2.38 Å resolution. The catalytic entity reveals an α/β short chain alcohol dehydrogenase/reductase (SDR) fold and the conformation of the bound nicotinamide adenine dinucleotide (NAD +) found in other SDR enzymes. Of great interest is the separate COOH-terminal domain, which is not seen in other SDR structures. This domain completes the active site cavity of the neighboring monomer and extends dimeric interactions. Peroxisomal diseases that arise because of point mutations in the dehydrogenase-coding region of the MFE-2 gene can be mapped to changes in amino acids involved in NAD + binding and protein dimerization.
ISSN:0969-2126
1878-4186
DOI:10.1016/S0969-2126(02)00931-0