Hammond Robert G, Tan Xuan, Johnson Margaret A
Department of Chemistry, University of Alabama at Birmingham, Birmingham, Alabama, 35294.
Protein Sci. 2017 Sep;26(9):1726-1737. doi: 10.1002/pro.3208. Epub 2017 Jun 15.
The coronavirus nonstructural protein 3 (nsp3) is a multifunctional protein that comprises multiple structural domains. This protein assists viral polyprotein cleavage, host immune interference, and may play other roles in genome replication or transcription. Here, we report the solution NMR structure of a protein from the "SARS-unique region" of the bat coronavirus HKU9. The protein contains a frataxin fold or double-wing motif, which is an α + β fold that is associated with protein/protein interactions, DNA binding, and metal ion binding. High structural similarity to the human severe acute respiratory syndrome (SARS) coronavirus nsp3 is present. A possible functional site that is conserved among some betacoronaviruses has been identified using bioinformatics and biochemical analyses. This structure provides strong experimental support for the recent proposal advanced by us and others that the "SARS-unique" region is not unique to the human SARS virus, but is conserved among several different phylogenetic groups of coronaviruses and provides essential functions.
冠状病毒非结构蛋白3（nsp3）是一种多功能蛋白，包含多个结构域。该蛋白协助病毒多聚蛋白切割、干扰宿主免疫，并且可能在基因组复制或转录中发挥其他作用。在此，我们报道了来自蝙蝠冠状病毒HKU9“非典独特区域”一种蛋白的溶液核磁共振结构。该蛋白含有一个铁硫蛋白折叠或双翼基序，这是一种与蛋白质/蛋白质相互作用、DNA结合和金属离子结合相关的α + β折叠。它与人类严重急性呼吸综合征（SARS）冠状病毒nsp3具有高度的结构相似性。通过生物信息学和生化分析，已确定了一些β冠状病毒中保守的一个可能功能位点。该结构为我们和其他人最近提出的观点提供了有力的实验支持，即“非典独特”区域并非人类SARS病毒所特有，而是在几种不同系统发育组的冠状病毒中保守，并发挥着重要功能。
