Structural polymorphism of the Escherichia coli poly-α-L-glutamate synthetase RimK
Structural polymorphism of the Escherichia coli poly-α-L-glutamate synthetase RimK
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DOI：
10.1107/s2053230x18007689
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发表时间：
2018-07-01
影响因子：
0.9
通讯作者：
Kurumizaka, Hitoshi
中科院分区：
文献类型：
--
作者：
Arimura, Yasuhiro;Kono, Tomonori;Kurumizaka, Hitoshi
细菌RimK是一种催化核糖体蛋白S6的C-末端的聚谷氨酰化和使用L-谷氨酸合成聚-α-L-谷氨酸肽的酶。在本研究中，在2.05埃分辨率下测定了与ATP类似物AMP-PNP复合的大肠杆菌RimK蛋白的晶体结构。在晶体中观察到两种不同构象的RimK，封闭和开放形式。本研究揭示的结构多态性为理解RimK催化聚α-L-谷氨酸肽合成和核糖体蛋白S6聚谷氨酰化的机制提供了重要信息。
Bacterial RimK is an enzyme that catalyzes the polyglutamylation of the C-terminus of ribosomal protein S6 and the synthesis of poly-alpha-L-glutamate peptides using l-glutamic acid. In the present study, the crystal structure of the Escherichia coli RimK protein complexed with the ATP analogue AMP-PNP was determined at 2.05 angstrom resolution. Two different conformations of RimK, closed and open forms, were observed in the crystals. The structural polymorphism revealed in this study provided important information to understand the mechanism by which RimK catalyzes the synthesis of poly-alpha-L-glutamate peptides and the polyglutamylation of ribosomal protein S6.