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首页> 外文期刊>Acta crystallographica. Section D, Structural biology. >RNA protects a nucleoprotein complex against radiation damage
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RNA protects a nucleoprotein complex against radiation damage

机译：RNA保护核蛋白质复杂的反对辐射损伤

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摘要

Radiation damage during macromolecular X-ray crystallographic data collection is still the main impediment for many macromolecular structure determinations. Even when an eventual model results from the crystallographic pipeline, the manifestations of radiation-induced structural and conformation changes, the so-called specific damage, within crystalline macromolecules can lead to false interpretations of biological mechanisms. Although this has been well characterized within protein crystals, far less is known about specific damage effects within the larger class of nucleoprotein complexes. Here, a methodology has been developed whereby per-atom density changes could be quantified with increasing dose over a wide (1.3-25.0 MGy) range and at higher resolution (1.98 angstrom) than the previous systematic specific damage study on a protein-DNA complex. Specific damage manifestations were determined within the large trp RNA-binding attenuation protein (TRAP) bound to a single-stranded RNA that forms a belt around the protein. Over a large dose range, the RNAwas found to be far less susceptible to radiation-induced chemical changes than the protein. The availability of two TRAP molecules in the asymmetric unit, of which only one contained bound RNA, allowed a controlled investigation into the exact role of RNA binding in protein specific damage susceptibility. The 11-fold symmetry within each TRAP ring permitted statistically significant analysis of the Glu and Asp damage patterns, with RNA binding unexpectedly being observed to protect these otherwise highly sensitive residues within the 11 RNA-binding pockets distributed around the outside of the protein molecule. Additionally, the method enabled a quantification of the reduction in radiation-induced Lys and Phe disordering upon RNA binding directly from the electron density.
机译：在大分子x射线辐射损伤晶体数据收集仍然是许多大分子结构主要障碍决定。结果从晶体管道辐射诱导的表现结构和构象变化,所谓的具体损坏,在水晶大分子可以导致错误的解释的生物机制。在蛋白质晶体的特点,要少得多众所周知中的特定损害的影响呢更大的核蛋白质复合物类。方法已经被开发出来,每个原子密度的变化可以量化增加剂量(1.3 - -25.0 MGy)范围宽在高分辨率(1.98埃)比以前的系统具体的损伤研究protein-DNA复杂。在大型表现确定衰减trp rna结合蛋白(陷阱)单链RNA组成一个皮带的蛋白质。发现更容易辐射诱导的化学变化蛋白质。在不对称单位,其中只有一个包含绑定RNA,允许控制调查RNA的确切角色绑定在蛋白质特定损伤易感性。11-fold对称环允许在每个陷阱统计上显著的Glu和分析Asp破坏模式,与RNA绑定保护这些意外被观测到否则11内残留高度敏感rna结合分布式在口袋里外的蛋白质分子。启用的量化方法减少辐射诱导赖氨酸和板式换热器直接从无序化在RNA绑定电子密度。

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