Abstract

Multifunctional enzyme type 2 (MFE-2) forms part of the fatty acid b-oxidation pathway in peroxisomes.MFE-2s from various species reveal proteins with structurally homologous functionaldomains assembled in different compilations. Crystal structures of all domain types are known.SAXS data from human, fruit fly and Caenorhabditis elegans MFE-2s and their constituent domainswere collected, and both ab initio and rigid body models constructed. Location of the putative substratebinding helper domain SCP-2L (sterol carrier protein 2-like), which is not part of MFE-2 proteinin every species and not seen as part of any previous MFE-2 structures, was determined. Theobtained models of human and C. elegans MFE-2 lend a direct structural support to the idea ofthe biological role of SCP-2L

    Similar works