1ZCJ

Crystal structure of 3-hydroxyacyl-CoA dehydrogenase

Summary for 1ZCJ

• Entry DOI: 10.2210/pdb1zcj/pdb
• Descriptor: Peroxisomal bifunctional enzyme (2 entities in total)
• Functional Keywords: peroxisomal multifunctional enzyme type 1, rat, l-bifunctional enzyme, mfe-1, fatty acid beta oxidation, oxidoreductase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Peroxisome: P07896
• Total number of polymer chains: 1
• Total formula weight: 50939.29

Authors

Taskinen, J.P.,Kiema, T.R.,Hiltunen, J.K.,Wierenga, R.K. (deposition date: 2005-04-12, release date: 2006-01-10, Last modification date: 2023-10-25)

Primary citation

Taskinen, J.P.,Kiema, T.R.,Hiltunen, J.K.,Wierenga, R.K.
Structural Studies of MFE-1: the 1.9A Crystal Structure of the Dehydrogenase Part of Rat Peroxisomal MFE-1
J.Mol.Biol., 355:734-746, 2006

PubMed Abstract: The 1.9 A structure of the C-terminal dehydrogenase part of the rat peroxisomal monomeric multifunctional enzyme type 1 (MFE-1) has been determined. In this construct (residues 260-722 and referred to as MFE1-DH) the N-terminal hydratase part of MFE-1 has been deleted. The structure of MFE1-DH shows that it consists of an N-terminal helix, followed by a Rossmann-fold domain (domain C), followed by two tightly associated helical domains (domains D and E), which have similar topology. The structure of MFE1-DH is compared with the two known homologous structures: human mitochondrial 3-hydroxyacyl-CoA dehydrogenase (HAD; sequence identity is 33%) (which is dimeric and monofunctional) and with the dimeric multifunctional alpha-chain (alphaFOM; sequence identity is 28%) of the bacterial fatty acid beta-oxidation alpha2beta2-multienzyme complex. Like MFE-1, alphaFOM has an N-terminal hydratase part and a C-terminal dehydrogenase part, and the structure comparisons show that the N-terminal helix of MFE1-DH corresponds to the alphaFOM linker helix, located between its hydratase and dehydrogenase part. It is also shown that this helix corresponds to the C-terminal helix-10 of the hydratase/isomerase superfamily, suggesting that functionally it belongs to the N-terminal hydratase part of MFE-1.

PubMed: 16330050
DOI: 10.1016/j.jmb.2005.10.085

Experimental method

X-RAY DIFFRACTION (1.9 Å)