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TitleQuaternary structure of human, Drosophila melanogaster and Caenorhabditis elegans MFE-2 in solution from synchrotron small-angle X-ray scattering.
Journal, issue, pagesFEBS Lett, Vol. 587, Issue 4, Page 305-310, Year 2013
Publish dateFeb 14, 2013
AuthorsMaija L Mehtälä / Tatu J K Haataja / Clément E Blanchet / J Kalervo Hiltunen / Dmitri I Svergun / Tuomo Glumoff /
PubMed AbstractMultifunctional enzyme type 2 (MFE-2) forms part of the fatty acid β-oxidation pathway in peroxisomes. MFE-2s from various species reveal proteins with structurally homologous functional domains ...Multifunctional enzyme type 2 (MFE-2) forms part of the fatty acid β-oxidation pathway in peroxisomes. MFE-2s from various species reveal proteins with structurally homologous functional domains assembled in different compilations. Crystal structures of all domain types are known. SAXS data from human, fruit fly and Caenorhabditiselegans MFE-2s and their constituent domains were collected, and both ab initio and rigid body models constructed. Location of the putative substrate binding helper domain SCP-2L (sterol carrier protein 2-like), which is not part of MFE-2 protein in every species and not seen as part of any previous MFE-2 structures, was determined. The obtained models of human and C. elegans MFE-2 lend a direct structural support to the idea of the biological role of SCP-2L.
External linksFEBS Lett / PubMed:23313254
MethodsSAS (X-ray synchrotron)
Structure data

SASDAF4: DmMfe2 (Peroxisomal multifunctional enzyme type 2)
Method: SAXS/SANS

SASDAG4: HsMfe2 (Peroxisomal multifunctional enzyme type 2)
Method: SAXS/SANS

Source
  • Drosophila melanogaster (fruit fly)
  • Homo sapiens (human)

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