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首页> 外文期刊>Journal of Molecular Biology >SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA binding.
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SARS coronavirus unique domain: three-domain molecular architecture in solution and RNA binding.

机译：SARS冠状病毒的独特结构域：溶液中的三结构域分子结构与RNA结合。

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摘要

Nonstructural protein 3 of the severe acute respiratory syndrome (SARS) coronavirus includes a "SARS-unique domain" (SUD) consisting of three globular domains separated by short linker peptide segments. This work reports NMR structure determinations of the C-terminal domain (SUD-C) and a two-domain construct (SUD-MC) containing the middle domain (SUD-M) and the C-terminal domain, and NMR data on the conformational states of the N-terminal domain (SUD-N) and the SUD-NM two-domain construct. Both SUD-N and SUD-NM are monomeric and globular in solution; in SUD-NM, there is high mobility in the two-residue interdomain linking sequence, with no preferred relative orientation of the two domains. SUD-C adopts a frataxin like fold and has structural similarity to DNA-binding domains of DNA-modifying enzymes. The structures of both SUD-M (previously determined) and SUD-C (from the present study) are maintained in SUD-MC, where the two domains are flexibly linked. Gel-shift experiments showed that both SUD-C and SUD-MC bind to single-stranded RNA and recognize purine bases more strongly than pyrimidine bases, whereby SUD-MC binds to a more restricted set of purine-containing RNA sequences than SUD-M. NMR chemical shift perturbation experiments with observations of (15)N-labeled proteins further resulted in delineation of RNA binding sites (i.e., in SUD-M, a positively charged surface area with a pronounced cavity, and in SUD-C, several residues of an anti-parallel beta-sheet). Overall, the present data provide evidence for molecular mechanisms involving the concerted actions of SUD-M and SUD-C, which result in specific RNA binding that might be unique to the SUD and, thus, to the SARS coronavirus.
机译：严重急性呼吸系统综合症（SARS）冠状病毒的非结构蛋白3包括“ SARS唯一域”（SUD），该域由由短接头肽段分隔的三个球状域组成。这项工作报告了C末端结构域（SUD-C）和包含中间结构域（SUD-M）和C末端结构域的两结构域构建体（SUD-MC）的NMR结构测定，以及有关构象的NMR数据N-末端结构域（SUD-N）和SUD-NM两结构域构建体的状态。 SUD-N和SUD-NM在溶液中均为单体和球状。在SUD-NM中，在两个残基的域间连接序列中具有高迁移率，而两个域没有优选的相对取向。 SUD-C具有类似frataxin的折叠，并且与DNA修饰酶的DNA结合结构域具有结构相似性。 SUD-M（先前确定）和SUD-C（根据本研究）的结构都保留在SUD-MC中，其中两个域可以灵活地链接。凝胶位移实验表明，SUD-C和SUD-MC均与单链RNA结合，并且比嘧啶碱基更能识别嘌呤碱基，因此SUD-MC与SUD-M结合更受限的含嘌呤RNA序列。核磁共振化学位移扰动实验，观察到（15）N标记的蛋白质，进一步确定了RNA结合位点（即在SUD-M中，带有明显空腔的带正电的表面积，在SUD-C中，存在多个残基）反平行的Beta版）。总体而言，本数据为涉及SUD-M和SUD-C协同作用的分子机制提供了证据，这些分子机制可导致SUD特有的特异性RNA结合，从而对SARS冠状病毒具有独特性。

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