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7Y38

Molecular architecture of the chikungunya virus replication complex

Summary for 7Y38
Entry DOI10.2210/pdb7y38/pdb
EMDB information30796 33591
DescriptormRNA-capping enzyme nsP1,affinity-tag (strepII-3XFLAG), RNA-directed RNA polymerase nsP4, Protease nsP2, ... (7 entities in total)
Functional Keywordsreplicase, replication complex, viral rna replication, capping, helicase, protease, rna-dependent rna polymerase, rdrp, viral protein, viral protein-rna complex, viral protein/rna
Biological sourceChikungunya virus strain S27-African prototype
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Total number of polymer chains15
Total formula weight943964.21
Authors
Tan, Y.B.,Luo, D. (deposition date: 2022-06-10, release date: 2022-12-14, Last modification date: 2024-07-03)
Primary citationTan, Y.B.,Chmielewski, D.,Law, M.C.Y.,Zhang, K.,He, Y.,Chen, M.,Jin, J.,Luo, D.
Molecular architecture of the Chikungunya virus replication complex.
Sci Adv, 8:eadd2536-eadd2536, 2022
Cited by
PubMed Abstract: To better understand how positive-strand (+) RNA viruses assemble membrane-associated replication complexes (RCs) to synthesize, process, and transport viral RNA in virus-infected cells, we determined both the high-resolution structure of the core RNA replicase of chikungunya virus and the native RC architecture in its cellular context at subnanometer resolution, using in vitro reconstitution and in situ electron cryotomography, respectively. Within the core RNA replicase, the viral polymerase nsP4, which is in complex with nsP2 helicase-protease, sits in the central pore of the membrane-anchored nsP1 RNA-capping ring. The addition of a large cytoplasmic ring next to the C terminus of nsP1 forms the holo-RNA-RC as observed at the neck of spherules formed in virus-infected cells. These results represent a major conceptual advance in elucidating the molecular mechanisms of RNA virus replication and the principles underlying the molecular architecture of RCs, likely to be shared with many pathogenic (+) RNA viruses.
PubMed: 36449616
DOI: 10.1126/sciadv.add2536
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.8 Å)
Structure validation

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PDB entries from 2024-11-13

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