title: Structural determinants for phosphatidylinositol recognition by Sfh3 and substrate-induced dimer-monomer transition during lipid transfer cycles.
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.
authors.affiliation: College of Pharmacy, Chonnam National University, Gwangju 500-757, South Korea.
authors.forename: Huiseon
authors.initials: H
authors.lastname: Yang
authors.forename: Junsen
authors.initials: J
authors.lastname: Tong
authors.forename: Thomas A
authors.initials: TA
authors.lastname: Leonard
authors.forename: Young Jun
authors.initials: YJ
authors.lastname: Im
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010716:Phosphatidylinositols / Q000737:chemistry*; D049294:Phospholipid Transfer Proteins / Q000737:chemistry*; D011485:Protein Binding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D013379:Substrate Specificity
chemical_list: C483431:PDR16 protein, S cerevisiae; D010716:Phosphatidylinositols; D049294:Phospholipid Transfer Proteins; D029701:Saccharomyces cerevisiae Proteins