1zcj
From Proteopedia
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Crystal structure of 3-hydroxyacyl-CoA dehydrogenase
Overview
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.
About this Structure
1ZCJ is a Single protein structure of sequence from Rattus norvegicus. Active as 3-hydroxyacyl-CoA dehydrogenase, with EC number 1.1.1.35 Full crystallographic information is available from OCA.
Reference
Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1., Taskinen JP, Kiema TR, Hiltunen JK, Wierenga RK, J Mol Biol. 2006 Jan 27;355(4):734-46. Epub 2005 Nov 18. PMID:16330050
Page seeded by OCA on Wed Nov 21 07:23:04 2007
