Search and Subvert: Minimalist Bacterial Phosphatidylinositol-Specific Phospholipase C Enzymes

Chemical Reviews
Mary F RobertsAnne Gershenson

Abstract

Phosphatidylinositol-specific phospholipase C (PI-PLC) enzymes from Gram-positive bacteria are secreted virulence factors that aid in downregulating host immunity. These PI-PLCs are minimalist peripheral membrane enzymes with a distorted (βα)8 TIM barrel fold offering a conserved and stable scaffold for the conserved catalytic amino acids while membrane recognition is achieved mostly through variable loops. Decades of experimental and computational research on these enzymes have revealed the subtle interplay between molecular mechanisms of catalysis and membrane binding, leading to a semiquantitative model for how they find, bind, and cleave their respective substrates on host cell membranes. Variations in sequence and structure of their membrane binding sites may correlate with how enzymes from different Gram-positive bacteria search for their particular targets on the membrane. Detailed molecular characterization of protein-lipid interactions have been aided by cutting-edge methods ranging from 31P field-cycling NMR relaxometry to monitor protein-induced changes in phospholipid dynamics to molecular dynamics simulations to elucidate the roles of electrostatic and cation-π interactions in lipid binding to single molecule fluor...Continue Reading

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Citations

Aug 28, 2020·Essays in Biochemistry·Matilda Katan, Shamshad Cockcroft
Mar 27, 2020·The Journal of Cell Biology·Joshua G PembertonTamas Balla
Jun 11, 2020·The Journal of Biological Chemistry·Julius CampeciñoEric L Hegg
Sep 24, 2020·Progress in Lipid Research·Matilda Katan, Shamshad Cockcroft
Feb 26, 2020·Journal of Chemical Theory and Computation·Hanif M KhanNathalie Reuter
Oct 2, 2020·Biochimica Et Biophysica Acta. Biomembranes·Anna S AlekseevaIvan A Boldyrev

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