EMD-32914

Single-particle
2.62 Å
EMD-32914 Deposition: 20/02/2022
Map released: 10/08/2022
Last modified: 26/06/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-32914

Cryo-EM Structure of Chikungunya Virus Nonstructural Protein 1 with inhibitor FHA

EMD-32914

Single-particle
2.62 Å
EMD-32914 Deposition: 20/02/2022
Map released: 10/08/2022
Last modified: 26/06/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Chikungunya virus strain S27-African prototype
Sample: Nonstructural Protein 1
Fitted models: 7x01 (Avg. Q-score: 0.599)

Deposition Authors: Zhang K, Law MCY
Molecular basis of specific viral RNA recognition and 5'-end capping by the Chikungunya virus nsP1.
Zhang K, Law MCY, Nguyen TM, Tan YB, Wirawan M, Law YS, Jeong LS, Luo D
(2022) Cell Rep , 40 , 111133 - 111133
PUBMED: 35905713
DOI: doi:10.1016/j.celrep.2022.111133
ISSN: 2211-1247
Abstract:
Many viruses encode RNA-modifying enzymes to edit the 5' end of viral RNA to mimic the cellular mRNA for effective protein translation, genome replication, and evasion of the host defense mechanisms. Alphavirus nsP1 synthesizes the 5' end Cap-0 structure of viral RNAs. However, the molecular basis of the capping process remains unclear. We determine high-resolution cryoelectron microscopy (cryo-EM) structures of Chikungunya virus nsP1 in complex with m7GTP/SAH, covalently attached m7GMP, and Cap-0 viral RNA. These structures reveal details of viral-RNA-capping reactions and uncover a sequence-specific virus RNA-recognition pattern that, in turn, regulates viral-RNA-capping efficiency to ensure optimal genome replication and subgenomic RNA transcription. This sequence-specific enzyme-RNA pairing is conserved across all alphaviruses.