Correction: Structural basis of phosphatidylcholine recognition by the C2-Domain of cytosolic phospholipase A2α

Hirano, Yoshinori; Gao, Yong-Guang; Stephenson, Daniel J.; Vu, Ngoc; Malinina, Lucy; Simanshu, Dhirendra K.; Chalfant, Charles E.; Patel, Dinshaw J.; Brown, Rhoderick E.

doi:10.7554/elife.75278

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“…So far, there are only a few other peripheral membrane proteins where PC-cation–aromatic Tyr/Trp/Phe complexes have been identified and shown to be important for membrane binding. These include a number of phospholipases in addition to Bt PI-PLC: the cytosolic phospholipase A 2 , whose C 2 domain forms a PC-cation–Tyr-π complex that is also stabilized by a Ca +2 interacting with the lipid phosphate group [ 33 ]; phospholipase A 2 Naja naja atra , where ΔΔG data are available for replacing aromatic amino acids by Ala [ 34 ], and the PC specificity was shown to arise from cation-π complexes by simulations [ 26 ]; and a spider phospholipase D that uses Tyr cages around the bound PC cation [ 35 ]. The PC cation-π formation in the PLD appears conserved in many of the other members in the same clade, emphasizing these are distinct complexes that are useful for ensuring PC specificity.…”

Section: Discussionmentioning

confidence: 99%

Phosphatidylcholine Cation—Tyrosine π Complexes: Motifs for Membrane Binding by a Bacterial Phospholipase C

2022

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Phosphatidylinositol-specific phospholipase C (PI-PLC) enzymes are a virulence factor in many Gram-positive organisms. The specific activity of the Bacillus thuringiensis PI-PLC is significantly increased by adding phosphatidylcholine (PC) to vesicles composed of the substrate phosphatidylinositol, in part because the inclusion of PC reduces the apparent Kd for the vesicle binding by as much as 1000-fold when comparing PC-rich vesicles to PI vesicles. This review summarizes (i) the experimental work that localized a site on BtPI-PLC where PC is bound as a PC choline cation—Tyr-π complex and (ii) the computational work (including all-atom molecular dynamics simulations) that refined the original complex and found a second persistent PC cation—Tyr-π complex. Both complexes are critical for vesicle binding. These results have led to a model for PC functioning as an allosteric effector of the enzyme by altering the protein dynamics and stabilizing an ‘open’ active site conformation.

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