期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 113, 期 28, 页码 E4005-E4014出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1602591113
关键词
RNA-dependent RNA polymerase; nucleotide addition cycle; translocation intermediate; enterovirus 71; crystal structure
资金
- National Key Basic Research Program of China [2013CB911100]
- National Natural Science Foundation of China [31370198]
- Hundred Talents Program of the Chinese Academy of Sciences
Viral RNA-dependent RNA polymerases (RdRPs) play essential roles in viral genome replication and transcription. We previously reported several structural states of the poliovirus RdRP nucleotide addition cycle (NAC) that revealed a unique palm domain-based active site closure mechanism and proposed a six-state NAC model including a hypothetical state representing translocation intermediates. Using the RdRP from another human enterovirus, enterovirus 71, here we report seven RdRP elongation complex structures derived from a crystal lattice that allows three NAC events. These structures suggested a key order of events in initial NTP binding and NTP-induced active site closure and revealed a bona fide translocation intermediate featuring asymmetric movement of the template-product duplex. Our work provides essential missing links in understanding NTP recognition and translocation mechanisms in viral RdRPs and emphasizes the uniqueness of the viral RdRPs compared with other processive polymerases.
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