Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
J Mol Biol. 2010 Oct 1;402(4):619-28. doi: 10.1016/j.jmb.2010.07.043. Epub 2010 Aug 13.
The NMR structure of the severe acute respiratory syndrome coronavirus nonstructural protein (nsp) 7 in aqueous solution at pH 6.5 was determined and compared with the results of previous structure determinations of nsp7 in solution at pH 7.5 and in the crystals of a hexadecameric nsp7/nsp8 complex obtained from a solution at pH 7.5. All three structures contain four helices as the only regular secondary structures, but there are differences in the lengths and sequence locations of the four helices, as well as between the tertiary folds. The present study includes data on conformational equilibria and intramolecular rate processes in nsp7 in solution at pH 6.5, which provide further insights into the polymorphisms implicated by a comparison of the three presently available nsp7 structures.
在 pH 值为 6.5 的水溶液中测定了严重急性呼吸综合征冠状病毒非结构蛋白(nsp)7 的 NMR 结构,并与之前在 pH 值为 7.5 的溶液中和在 pH 值为 7.5 的溶液中获得的十六聚体 nsp7/nsp8 复合物晶体中 nsp7 的结构测定结果进行了比较。这三个结构都包含四个螺旋作为唯一的规则二级结构,但四个螺旋的长度和序列位置以及三级折叠存在差异。本研究包括 pH 值为 6.5 的溶液中 nsp7 的构象平衡和分子内速率过程的数据,这为通过比较目前可用的三个 nsp7 结构来研究所涉及的多态性提供了进一步的见解。