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Structural determinants for phosphatidylinositol recognition by Sfh3 and substrate‐induced dimer–monomer transition during lipid transfer cycles
Author(s) -
Yang Huiseon,
Tong Junsen,
Leonard Thomas A.,
Im Young Jun
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.04.009
Subject(s) - phosphatidylinositol , dimer , monomer , substrate (aquarium) , chemistry , transition (genetics) , biophysics , biochemistry , biology , organic chemistry , signal transduction , polymer , ecology , gene
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.