Crystal structure of Middle East respiratory syndrome coronavirus helicase

PLoS Pathogens

Ivan Zlatev¹  Muthiah Manoharan¹  Rajat Das¹  Rong Zhao²  Ruiyun Han²  Wei Hao²  Sheng Cui²  Meitian Wang³  Justyna Aleksandra Wojdyla³ 

[1] Alnylam Pharmaceuticals, Cambridge, MA, United States of America;MOH key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, No.9 Dong Dan San Tiao, Beijing, China;Swiss Light Source at Paul Scherrer Institute, Villigen, Switzerland

关键词: Coronaviruses;    Helicases;    Crystal structure;    Zinc;    Sequence alignment;    Adenosine triphosphatase;    Multiple alignment calculation;    Sequence motif analysis;   

DOI  :  10.1371/journal.ppat.1006474

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

Middle East respiratory syndrome coronavirus (MERS-CoV) remains a threat to public health worldwide; however, effective vaccine or drug against CoVs remains unavailable. CoV helicase is one of the three evolutionary most conserved proteins in nidoviruses, thus making it an important target for drug development. We report here the first structure of full-length coronavirus helicase, MERS-CoV nsp13. MERS-CoV helicase has multiple domains, including an N-terminal Cys/His rich domain (CH) with three zinc atoms, a beta-barrel domain and a C-terminal SF1 helicase core with two RecA-like subdomains. Our structural analyses show that while the domain organization of nsp13 is conserved throughout nidoviruses, the individual domains of nsp13 are closely related to the equivalent eukaryotic domains of Upf1 helicases. The most distinctive feature differentiating CoV helicases from eukaryotic Upf1 helicases is the interaction between CH domain and helicase core.

【 授权许可】

CC BY