4J7Q

Crystal structure of Saccharomyces cerevisiae Sfh3 complexed with phosphatidylinositol

Summary for 4J7Q

• Entry DOI: 10.2210/pdb4j7q/pdb
• Descriptor: Phosphatidylinositol transfer protein PDR16, (1R)-2-{[(S)-hydroxy{[(1S,2R,3R,4S,5S,6R)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}-1-[(octadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate (3 entities in total)
• Functional Keywords: sec14 scaffold, lipid transport, phosphatidylinositol
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Lipid droplet: P53860
• Total number of polymer chains: 2
• Total formula weight: 78939.17

Authors

Yang, H.,Im, Y.J. (deposition date: 2013-02-14, release date: 2013-07-03, Last modification date: 2024-03-20)

Primary citation

Yang, H.,Tong, J.,Leonard, T.A.,Im, Y.J.
Structural determinants for phosphatidylinositol recognition by Sfh3 and substrate-induced dimer-monomer transition during lipid transfer cycles.
Febs Lett., 587:1610-1616, 2013

PubMed Abstract: Sec14 family homologs are the major yeast phosphatidylinositol/phosphatidylcholine transfer proteins regulating lipid metabolism and vesicle trafficking. The structure of Saccharomyces cerevisiae Sfh3 displays a conserved Sec14 scaffold and reveals determinants for the specific recognition of phosphatidylinositol ligand. Apo-Sfh3 forms a dimer through the hydrophobic interaction of gating helices. Binding of phosphatidylinositol leads to dissociation of the dimer into monomers in a reversible manner. This study suggests that the substrate induced dimer-monomer transformation is an essential part of lipid transfer cycles by Sfh3.

PubMed: 23603387
DOI: 10.1016/j.febslet.2013.04.009

Experimental method

X-RAY DIFFRACTION (1.55 Å)