Phosphatidylcholine Cation-Tyrosine π Complexes: Motifs for Membrane Binding by a Bacterial Phospholipase C.
Phosphatidylcholine Cation-Tyrosine π Complexes: Motifs for Membrane Binding by a Bacterial Phospholipase C.
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DOI：
10.3390/molecules27196184
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发表时间：
2022-09-21
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磷脂酰肌醇特异性磷脂酶C(PI-PLC)酶是许多革兰氏阳性菌的致病因子。通过将磷脂酰胆碱(PC)添加到由底物磷脂酰肌醇组成的囊泡中，苏云金芽孢杆菌PI-PLC的比活性显著提高，部分原因是当比较富含PC的囊泡和PI囊泡时，PC的加入使囊泡结合的表观Kd值降低了1000倍。本文综述了(I)将PC定位为PC胆碱阳离子-Tyr-π络合物的实验工作，以及(Ii)改进原始络合物并发现第二个持久的PC阳离子-Tyr-π络合物的计算工作(包括全原子分子动力学模拟)。这两种络合物都是囊泡结合的关键。这些结果导致了PC作为酶的变构效应器的模型，通过改变蛋白质动力学和稳定‘开放’活性部位构象。
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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