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7CXM

Architecture of a SARS-CoV-2 mini replication and transcription complex

Summary for 7CXM
Entry DOI10.2210/pdb7cxm/pdb
EMDB information30492
DescriptorRNA-directed RNA polymerase, Non-structural protein 8, Non-structural protein 7, ... (8 entities in total)
Functional Keywordssars-cov-2, rtc complex, viral protein-rna complex, viral protein/rna
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV)
More
Total number of polymer chains9
Total formula weight324119.80
Authors
Yan, L.,Zhang, Y.,Ge, J.,Zheng, L.,Gao, Y.,Wang, T.,Jia, Z.,Wang, H.,Huang, Y.,Li, M.,Wang, Q.,Rao, Z.,Lou, Z. (deposition date: 2020-09-02, release date: 2020-11-04, Last modification date: 2024-03-27)
Primary citationYan, L.,Zhang, Y.,Ge, J.,Zheng, L.,Gao, Y.,Wang, T.,Jia, Z.,Wang, H.,Huang, Y.,Li, M.,Wang, Q.,Rao, Z.,Lou, Z.
Architecture of a SARS-CoV-2 mini replication and transcription complex.
Nat Commun, 11:5874-5874, 2020
Cited by
PubMed Abstract: Non-structural proteins (nsp) constitute the SARS-CoV-2 replication and transcription complex (RTC) to play a pivotal role in the virus life cycle. Here we determine the atomic structure of a SARS-CoV-2 mini RTC, assembled by viral RNA-dependent RNA polymerase (RdRp, nsp12) with a template-primer RNA, nsp7 and nsp8, and two helicase molecules (nsp13-1 and nsp13-2), by cryo-electron microscopy. Two groups of mini RTCs with different conformations of nsp13-1 are identified. In both of them, nsp13-1 stabilizes overall architecture of the mini RTC by contacting with nsp13-2, which anchors the 5'-extension of RNA template, as well as interacting with nsp7-nsp8-nsp12-RNA. Orientation shifts of nsp13-1 results in its variable interactions with other components in two forms of mini RTC. The mutations on nsp13-1:nsp12 and nsp13-1:nsp13-2 interfaces prohibit the enhancement of helicase activity achieved by mini RTCs. These results provide an insight into how helicase couples with polymerase to facilitate its function in virus replication and transcription.
PubMed: 33208736
DOI: 10.1038/s41467-020-19770-1
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.9 Å)
Structure validation

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