title: Bacterial phosphatidylinositol-specific phospholipase C: structure, function, and interaction with lipids.
abstract: The bacterial phosphatidylinositol-specific phospholipase C (PI-PLC) is a small, water-soluble enzyme that cleaves the natural membrane lipids PI, lyso-PI, and glycosyl-PI. The crystal structure, NMR and enzymatic mechanism of bacterial PI-PLCs are reviewed. These enzymes consist of a single domain folded as a (betaalpha)(8)-barrel (TIM barrel), are calcium-independent, and interact weakly with membranes. Sequence similarity among PI-PLCs from different bacterial species is extensive, and includes the residues involved in catalysis. Bacterial PI-PLCs are structurally similar to the catalytic domain of mammalian PI-PLCs. Comparative studies of both prokaryotic and eukaryotic isozymes have proved useful for the identification of distinct regions of the proteins that are structurally and functionally important.
authors.affiliation: Institute of Molecular Biology and Department of Chemistry, University of Oregon, Eugene, OR 97403, USA. hayes@molbio.uoregon.edu
authors.forename: O H
authors.initials: OH
authors.lastname: Griffith
authors.forename: M
authors.initials: M
authors.lastname: Ryan
mesh_terms: D001419:Bacteria / Q000201:enzymology*; D001665:Binding Sites; D002384:Catalysis; D003460:Crystallization; D018360:Crystallography, X-Ray; D017261:Glycosylphosphatidylinositols / Q000378:metabolism; D050356:Lipid Metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D054801:Phosphoinositide Phospholipase C; D017385:Sequence Homology; D013329:Structure-Activity Relationship; D013379:Substrate Specificity; D010738:Type C Phospholipases / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D017261:Glycosylphosphatidylinositols; D010738:Type C Phospholipases; D054801:Phosphoinositide Phospholipase C; D043265:Phosphatidylinositol Diacylglycerol-Lyase