Structural highlights
Publication Abstract from PubMed
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.
Structural determinants for phosphatidylinositol recognition by Sfh3 and substrate-induced dimer-monomer transition during lipid transfer cycles.,Yang H, Tong J, Leonard TA, Im YJ FEBS Lett. 2013 Jun 5;587(11):1610-6. doi: 10.1016/j.febslet.2013.04.009. Epub, 2013 Apr 18. PMID:23603387[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yang H, Tong J, Leonard TA, Im YJ. Structural determinants for phosphatidylinositol recognition by Sfh3 and substrate-induced dimer-monomer transition during lipid transfer cycles. FEBS Lett. 2013 Jun 5;587(11):1610-6. doi: 10.1016/j.febslet.2013.04.009. Epub, 2013 Apr 18. PMID:23603387 doi:10.1016/j.febslet.2013.04.009
