原创力文档crystal structure of the c-terminal cytoplasmic domain of non-structural protein 4 from mouse hepatitis virus a59晶体结构的非结构性蛋白c端胞质域的4鼠肝炎病毒的事故.pdfVIP
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crystal structure of the c-terminal cytoplasmic domain of non-structural protein 4 from mouse hepatitis virus a59晶体结构的非结构性蛋白c端胞质域的4鼠肝炎病毒的事故
Crystal Structure of the C-Terminal Cytoplasmic Domain
of Non-Structural Protein 4 from Mouse Hepatitis Virus
A59
1 1 1 1,2 2 1,2
Xiaoling Xu , Zhiyong Lou , Yanlin Ma , Xuehui Chen , Zhangsheng Yang , Xiaohang Tong , Qi
1 1 2 3 1,2,3
Zhao , Yuanyuan Xu , Hongyu Deng , Mark Bartlam , Zihe Rao *
1 Laboratory of Structural Biology, Tsinghua University, Beijing, China, 2 National Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese Academy of
Sciences, Beijing, China, 3 College of Life Sciences and Tianjin Key Laboratory of Protein Science, Nankai University, Tianjin, China
Abstract
Background: The replication of coronaviruses takes place on cytoplasmic double membrane vesicles (DMVs) originating in
the endoplasmic reticulum (ER). Three trans-membrane non-structural proteins, nsp3, nsp4 and nsp6, are understood to be
membrane anchors of the coronavirus replication complex. Nsp4 is localized to the ER membrane when expressed alone
but is recruited into the replication complex in infected cells. It is revealed to contain four trans-membrane regions and its
N- and C-termini are exposed to the cytosol.
Methodology/Principal Findings: We have determined the crystal structures of the C-terminal hydrophilic domain of nsp4
(nsp4C) from MHV strain A59 and a C425S site-directed mutant. The highly conserved 89 amino acid region from T408 to
Q496 is shown to possess a new fold. The wild-type (WT) structure features two monomers linked by a Cys425-Cys425
di
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