6L1W

Zinc-finger Antiviral Protein (ZAP) bound to RNA

Summary for 6L1W

• Entry DOI: 10.2210/pdb6l1w/pdb
• Descriptor: Zinc finger CCCH-type antiviral protein 1, RNA (5'-R(*CP*GP*UP*CP*GP*U)-3'), ZINC ION, ... (4 entities in total)
• Functional Keywords: rna binding protein-rna complex, rna binding protein/rna
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 2
• Total formula weight: 28524.07

Authors

Luo, X.,Wang, X.,Gao, Y.,Zhu, J.,Liu, S.,Gao, G.,Gao, P. (deposition date: 2019-09-30, release date: 2020-01-01, Last modification date: 2023-11-22)

Primary citation

Luo, X.,Wang, X.,Gao, Y.,Zhu, J.,Liu, S.,Gao, G.,Gao, P.
Molecular Mechanism of RNA Recognition by Zinc-Finger Antiviral Protein.
Cell Rep, 30:46-52.e4, 2020

PubMed Abstract: Zinc-finger antiviral protein (ZAP) is a host antiviral factor that specifically restricts a wide range of viruses. ZAP selectively binds to CG-dinucleotide-enriched RNA sequences and recruits multiple RNA degradation machines to degrade target viral RNA. However, the molecular mechanism and structural basis for ZAP recognition of specific RNA are not clear. Here, we report the crystal structure of the ZAP N-terminal domain bound to a CG-rich single-stranded RNA, providing the molecular basis for its specific recognition of a CG dinucleotide and additional guanine and cytosine. The four zinc fingers of ZAP adopt a unique architecture and form extensive interactions with RNA. Mutations of both protein and RNA at the RNA-ZAP interacting surface reduce the in vitro binding affinity and cellular antiviral activity. This work reveals the molecular mechanism of ZAP recognition of specific target RNA and also provides insights into the mechanism by which ZAP coordinates downstream RNA degradation processes.

PubMed: 31914396
DOI: 10.1016/j.celrep.2019.11.116

Experimental method

X-RAY DIFFRACTION (2.194 Å)