4i9m

Structure of the N254Y/H258Y mutant of the phosphatidylinositol-specific phospholipase C from Staphylococcus aureus bound to HEPES

spinqualitylabelsall models 4i9m, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4i9m is a 1 chain structure with sequence from Staphylococcus aureus subsp. aureus str. Newman. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: EPE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PLC_STAAE Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates. Potential virulence factor. Publication Abstract from PubMed Peripheral membrane proteins can be targeted to specific organelles or the plasma membrane by differential recognition of phospholipid headgroups. Although molecular determinants of specificity for several headgroups, including phosphatidylserine and phosphoinositides are well defined, specific recognition of the headgroup of the zwitterionic phosphatidylcholine (PC) is less well understood. In cytosolic proteins the cation-pi box provides a suitable receptor for choline recognition and binding through the trimethylammonium moiety. In PC, this moiety might provide a sufficient handle to bind to peripheral proteins via a cation-pi cage, where the pi systems of two or more aromatic residues are within 4-5 A of the quaternary amine. We prove this hypothesis by engineering the cation-pi box into secreted phosphatidylinositol-specific phospholipase C from Staphylococcus aureus, which lacks specific PC recognition. The N254Y/H258Y variant selectively binds PC-enriched vesicles, and x-ray crystallography reveals N254Y/H258Y binds choline and dibutyroylphosphatidylcholine within the cation-pi motif. Such simple PC recognition motifs could be engineered into a wide variety of secondary structures providing a generally applicable method for specific recognition of PC. The cation-pi box is a specific phosphatidylcholine membrane targeting motif.,Cheng J, Goldstein R, Gershenson A, Stec B, Roberts MF J Biol Chem. 2013 May 24;288(21):14863-73. doi: 10.1074/jbc.M113.466532. Epub, 2013 Apr 10. PMID:23576432 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phospholipase C

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