4j7p
From Proteopedia
Crystal structure of Saccharomyces cerevisiae Sfh3
Structural highlights
FunctionPDR16_YEAST Has phosphatidylinositol transfer activity. Involved in the regulation of the phospholipid composition of plasma- and endomembranes. Altering plasma membrane composition may provide a possible mechanism for multidrug resistance. Involved in the regulation of sterol biosynthesis. Contributes to efficient phospholipase D1 activation in the regulation of phospholipid turnover.[1] [2] Publication Abstract from PubMedSec14 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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