Journal
SCIENCE ADVANCES
Volume 3, Issue 4, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.1602573
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Funding
- National Natural Science Foundation of China [81572005]
- National Key Research and Development Program of China [2016YFD0500300]
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Enterovirus 71 (EV71) is the major pathogen responsible for outbreaks of hand, foot, and mouth disease. EV71 nonstructural protein 2C participates inmany critical events throughout the virus life cycle; however, its precise role is not fully understood. Lack of a high- resolution structure made it difficult to elucidate 2C activity and prevented inhibitor development. We report the 2.5 A-resolution crystal structure of the soluble part of EV71 2C, containing an adenosine triphosphatase (ATPase) domain, a cysteine-rich zinc finger with an unusual fold, and a carboxyl-terminal helical domain. Unlike other AAA+ ATPases, EV71 2C undergoes a carboxyl terminus-mediated self- oligomerization, which is dependent on a specific interaction between the carboxyl- terminal helix of one monomer and a deep pocket formed between the ATPase and the zinc finger domains of the neighboringmonomer. The carboxyl terminus-mediated selfoligomerization is fundamental to 2C ATPase activity and EV71 replication. Our findings suggest a strategy for inhibition of enterovirus replication by disruption of the self-oligomerization interface of 2C.
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