7DOP
Structural insights into viral RNA capping and plasma membrane targeting by Chikungunya virus nonstructural protein 1
Summary for 7DOP
Entry DOI | 10.2210/pdb7dop/pdb |
EMDB information | 30796 |
Descriptor | Nonstructural Protein 1, ZINC ION (2 entities in total) |
Functional Keywords | nonstructural protein, chikungunya virus, rna cap, replication, membrane associations, viral protein |
Biological source | Chikungunya virus strain S27-African prototype (CHIKV) |
Total number of polymer chains | 12 |
Total formula weight | 745463.38 |
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 citation | Zhang, 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: 33730549DOI: 10.1016/j.chom.2021.02.018 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.38 Å) |
Structure validation
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