Staup Andrew J, De Silva Ivon U, Catt Justin T, Tan Xuan, Hammond Robert G, Johnson Margaret A
Department of Chemistry, 1720 2nd Avenue S. CHEM 201, University of Alabama at Birmingham, AL, USA.
Department of Chemistry, 1720 2nd Avenue S. CHEM 274, University of Alabama at Birmingham, AL, USA.
Nat Prod Commun. 2019 May 27;14(5):1934578X19849202. doi: 10.1177/1934578X19849202. eCollection 2019 May.
Coronaviruses (CoVs) that cause infections such as severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome phylogenetically originate from bat CoVs. The coronaviral nonstructural protein 3 (nsp3) has been implicated in viral replication, polyprotein cleavage, and host immune interference. We report the structure of the C domain from the SARS-Unique Domain of bat CoV HKU4. The protein has a frataxin fold, consisting of 5 antiparallel β strands packed against 2 α helices. Bioinformatics analyses and nuclear magnetic resonance experiments were conducted to investigate the function of HKU4 C. The results showed that HKU4 C engages in protein-protein interactions with the nearby M domain of nsp3. The HKU4 C residues involved in protein-protein interactions are conserved in group 2c CoVs, indicating a conserved function.
引起严重急性呼吸综合征（SARS）和中东呼吸综合征等感染的冠状病毒在系统发育上起源于蝙蝠冠状病毒。冠状病毒非结构蛋白3（nsp3）与病毒复制、多聚蛋白切割及宿主免疫干扰有关。我们报道了蝙蝠冠状病毒HKU4的SARS-独特结构域C结构域的结构。该蛋白具有铁硫蛋白折叠结构，由5条反平行β链与2条α螺旋堆积而成。进行了生物信息学分析和核磁共振实验以研究HKU4 C的功能。结果表明，HKU4 C与nsp3附近的M结构域发生蛋白质-蛋白质相互作用。参与蛋白质-蛋白质相互作用的HKU4 C残基在2c组冠状病毒中保守，表明其功能保守。
