Activation by Allostery in Cell-Wall Remodeling by a Modular Membrane-Bound LyticTransglycosylase from Pseudomonas aeruginosa
Activation by Allostery in Cell-Wall Remodeling by a Modular Membrane-Bound LyticTransglycosylase from Pseudomonas aeruginosa
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DOI：
10.1016/j.str.2016.07.019
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发表时间：
2016-10-04
期刊：
影响因子：
5.7
通讯作者：
Hermoso, Juan A.
中科院分区：
文献类型：
--
作者：
Dominguez-Gil, Teresa;Lee, Mijoon;Hermoso, Juan A.
细菌生长和分裂不会丧失细胞的完整性。这一成就是值得注意的，因为它们细胞包膜的关键成分是周围的糖肽聚合物。在革兰氏阴性细菌中，这种聚合物-肽聚糖-通过同时合成和降解之间的差异而生长。这些活动的酶系综的调节知之甚少。我们在此报告的结构基础控制这样的酶，裂解转糖基酶MltF的铜绿假单胞菌。其结构包括两个模块：ABC转运蛋白样调节模块和催化模块。由肽聚糖衍生的胞肽占据调节模块影响在整个蛋白质结构上发生的显著且长距离（40埃）的构象变化，以打开其活性位点用于催化。MltF催化的变构控制的分子基础的这一发现是进一步研究动态肽聚糖的复杂酶协调内的MltF的基础。
Bacteria grow and divide without loss of cellular integrity. This accomplishment is notable, as a key component of their cell envelope is a surrounding glycopeptide polymer. In Gram-negative bacteria this polymer-the peptidoglycan-grows by the difference between concurrent synthesis and degradation. The regulation of the enzymatic ensemble for these activities is poorly understood. We report herein the structural basis for the control of one such enzyme, the lytic transglycosylase MltF of Pseudomonas aeruginosa. Its structure comprises two modules: an ABC-transporter-like regulatory module and a catalytic module. Occupancy of the regulatory module by peptidoglycan-derived muro-peptides effects a dramatic and long-distance (40 angstrom) conformational change, occurring over the entire protein structure, to open its active site for catalysis. This discovery of the molecular basis for the allosteric control of MltF catalysis is foundational to further study of MltF within the complex enzymatic orchestration of the dynamic peptidoglycan.