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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Functionally important movements in RecA molecules and filaments: studies involving mutation and environmental changes.
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Functionally important movements in RecA molecules and filaments: studies involving mutation and environmental changes.

机译：功能的重要运动RecA分子丝:研究涉及突变和环境的变化。

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摘要

The crystal structures of mutants of Mycobacterium smegmatis RecA (MsRecA) involving changes of Gln196 from glutamine to alanine, asparagine and glutamic acid, wild-type MsRecA and several of their nucleotide complexes have been determined using mostly low-temperature and partly room-temperature X-ray data. At both temperatures, nucleotide binding results in a movement of Gln196 towards the bound nucleotide in the wild-type protein. This movement is abolished in the mutants, thus establishing the structural basis for the triggering action of the residue in terms of the size, shape and the chemical nature of the side chain. The 19 crystal structures reported here, together with 11 previously reported MsRecA structures, provide further elaboration of the relation between the pitch of the ;inactive' RecA filament, the orientation of the C-terminal domain with respect to the main domain and the location of the switch residue. The low-temperature structures define one extreme of the range of positions the C-terminal domain can occupy. The movement of the C-terminal domain is correlated with those of the LexA-binding loop and the loop that connects the main and the N-terminal domains. These elements of molecular plasticity are made use of in the transition to the ;active' filament, as evidenced by the recently reported structures of RecA-DNA complexes. The available structures of RecA resulting from X-ray and electron-microscopic studies appear to represent different stages in the trajectory of the allosteric transformations of the RecA filament. The work reported here contributes to the description of the early stages of this trajectory and provides insight into structures relevant to the later stages.
机译：分枝杆菌的突变体的晶体结构smegmatis RecA (MsRecA)的变化Gln196从谷氨酰胺、丙氨酸、天冬酰胺和谷氨酸,野生型MsRecA和几个的他们的核苷酸复合物已经确定使用主要是低温和部分室温的x射线数据。温度、核苷酸绑定结果运动Gln196向绑定核苷酸在野生型蛋白。废除的突变体,从而建立触发操作的结构基础残留的大小、形状和侧链的化学性质。结构报告,连同11之前报道MsRecA结构,提供之间的关系的进一步细化球场的;不活跃的RecA灯丝,取向的c端域与尊重主域和开关的位置残渣。一个极端的立场c端域可以占领。与c端域相关LexA-binding循环和循环连接主要和n端结构域。分子使用的可塑性过渡到;活跃的灯丝,就是明证最近报道RecA-DNA结构复合物。产生的x射线和电子显微镜研究似乎代表不同的阶段变构的轨迹转换RecA灯丝。有助于早期的描述阶段的轨迹,并提供洞察力到后期结构有关。

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