1GZ6

(3R)-HYDROXYACYL-COA DEHYDROGENASE FRAGMENT OF RAT PEROXISOMAL MULTIFUNCTIONAL ENZYME TYPE 2

Summary for 1GZ6

• Entry DOI: 10.2210/pdb1gz6/pdb
• Descriptor: ESTRADIOL 17 BETA-DEHYDROGENASE 4, SULFATE ION, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: dehydrogenase, 17beta-hsd4, mfe-2, beta-oxidation, peroxisome, sdr, steroid biosynthesis, oxidoreductase, nadp, multigene famil
• Biological source: RATTUS NORVEGICUS (RAT)
• Cellular location: Peroxisome: P97852
• Total number of polymer chains: 4
• Total formula weight: 142432.19

Authors

Haapalainen, A.M.,Hiltunen, J.K.,Glumoff, T. (deposition date: 2002-05-16, release date: 2003-01-24, Last modification date: 2011-07-13)

Primary citation

Haapalainen, A.M.,Koski, M.K.,Qin, Y.M.,Hiltunen, J.K.,Glumoff, T.
Binary Structure of the Two-Domain (3R)-Hydroxyacyl-Coa Dehydrogenase from Rat Peroxisomal Multifunctional Enzyme Type 2 at 2.38 A Resolution
Structure, 11:87-, 2003

PubMed Abstract: The crystal structure of (3R)-hydroxyacyl-CoA dehydrogenase of rat peroxisomal multifunctional enzyme type 2 (MFE-2) was solved at 2.38 A resolution. The catalytic entity reveals an alpha/beta 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.

PubMed: 12517343
DOI: 10.1016/S0969-2126(02)00931-0

Experimental method

X-RAY DIFFRACTION (2.38 Å)