Multifunctional enzyme type 2 (MFE-2) from rat

3-hydroxyacyl-CoA dehydrogenase domain

1GZ6

The dehydrogenase was found to consist of a typical Rossmann fold catalytic domain, but it also had a unique C-terminal 60-residue extension essential for dimerization and substrate binding.

Multifunctional enzyme type 2 (MFE-2) from Candida tropicalis

3-hydroxyacyl-CoA dehydrogenase domains A and B

2ET6

This yeast MFE-2 protein is exceptional, since it contains two dehydrogenase domains, which differ in substrate specificities: dehydrogenase A uses more readily longer chain lenght substrates than dehydrogenase B. 

Multifunctional enzyme type 2 (MFE-2) from Candida tropicalis and human

Enoyl-CoA hydratase 2 domain apoenzyme and complexed with (3R)-hydroxydecanoyl-CoA

1PN2, 1PN4 and 1S9C

The structures revealed a novel variation of the so called “hot dog” fold, which explained the structural basis for eukaryotic hydratase 2s being able to use long-chain substrates (contrary to corresponding bacterial enzymes): the ability is achieved by sacrificing one active site to create more binding space for bulkier substrates.

Multifunctional enzyme type 2 (MFE-2) from human

Sterol carrier protein-2 domain complexed with Triton X-100

1IKT

This domain is a non-specific lipid binding protein. It is part of some MFE-2 proteins, but not all, which raises the question of its role. Dynamic simulations of the structure with the bound ligand removed indicated that the C-terminal peroxisomal targeting signal is buried and not accessible if no ligand is bound.

Takaisin
Back