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7DOP

Structural insights into viral RNA capping and plasma membrane targeting by Chikungunya virus nonstructural protein 1

Summary for 7DOP
Entry DOI10.2210/pdb7dop/pdb
EMDB information30796
DescriptorNonstructural Protein 1, ZINC ION (2 entities in total)
Functional Keywordsnonstructural protein, chikungunya virus, rna cap, replication, membrane associations, viral protein
Biological sourceChikungunya virus strain S27-African prototype (CHIKV)
Total number of polymer chains12
Total formula weight745463.38
Authors
Zhang, K.,Law, Y.S.,Law, M.C.Y.,Tan, Y.B.,Wirawan, M.,Luo, D.H. (deposition date: 2020-12-15, release date: 2021-03-24, Last modification date: 2024-03-27)
Primary citationZhang, K.,Law, Y.S.,Law, M.C.Y.,Tan, Y.B.,Wirawan, M.,Luo, D.
Structural insights into viral RNA capping and plasma membrane targeting by Chikungunya virus nonstructural protein 1.
Cell Host Microbe, 29:757-, 2021
Cited by
PubMed Abstract: Chikungunya virus (CHIKV) causes a debilitating arthralgic inflammatory disease in humans. The multifunctional CHIKV protein, nsP1, facilitates virus RNA replication and transcription by anchoring the viral replication complex (RC) to plasma membrane vesicles and synthesizing the viral RNA 5' cap-0. Here, we report a cryo-EM structure of CHIKV nsP1 at 2.38 Å resolution. Twelve copies of nsP1 form a crown-shaped ring structure with a 7.5-nm-wide channel for mediating communication and exchange between the viral RC and the host cell. The catalytic site for viral RNA capping is located in a tunnel that is shaped by neighboring nsP1 molecules. Two membrane-association loops target nsP1 to the inner leaflet of the plasma membrane via palmitoylation and hydrophobic and electrostatic interactions. Our study provides the structural basis of viral RNA capping and RC assembly mediated by nsP1 and guides the development of antivirals targeting these essential steps of virus infection.
PubMed: 33730549
DOI: 10.1016/j.chom.2021.02.018
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.38 Å)
Structure validation

237735

数据于2025-06-18公开中

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