title: Dimeric Sfh3 has structural changes in its binding pocket that are associated with a dimer-monomer state transformation induced by substrate binding.
abstract: Phosphorylated derivatives of phosphatidylinositol (PtdIns), also called phosphoinositides (PIPs), are basic components of membrane-associated signalling systems. A family of PtdIns-transfer proteins (PITPs) called the Sec14 family have been predicted to form a set of functional modules that can sense different types of lipid metabolism and transmit the information to the PIP signalling system. In eukaryotic cells, the Sec14 family exhibits a wide diversity of activity, but the structural basis of this diversity remains unclear. In the present study, the dimeric structure of Sfh3 (Sec14 family homologue 3 in yeast) is reported for the first time and differs from the Sec14 proteins reported to date, all of which are monomeric. Some variations in the binding pocket of Sfh3 were observed and the dimer interface was identified and proposed to provide a link between dimer-monomer state changes and PtdIns binding. Together, these structural changes and the oligomeric state transformation of Sfh3 support ideas of diversity within the Sec14 family and provide some new clues to function.
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
authors.forename: Ye
authors.initials: Y
authors.lastname: Yuan
authors.forename: Wei
authors.initials: W
authors.lastname: Zhao
authors.forename: Xiao
authors.initials: X
authors.lastname: Wang
authors.forename: Yongxiang
authors.initials: Y
authors.lastname: Gao
authors.forename: Liwen
authors.initials: L
authors.lastname: Niu
authors.forename: Maikun
authors.initials: M
authors.lastname: Teng
mesh_terms: D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D050356:Lipid Metabolism / Q000502:physiology; D049294:Phospholipid Transfer Proteins / Q000737:chemistry / Q000378:metabolism / Q000502:physiology; D011485:Protein Binding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000502:physiology; D013379:Substrate Specificity
chemical_list: D049294:Phospholipid Transfer Proteins; D011994:Recombinant Proteins; C483438:SEC14 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins
keywords: Saccharomyces cerevisiae; Sfh3; dimer–monomer state change; homodimer