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crystal structure of alfalfa mosaic virus RNA 3'UTR in complex with coat protein N terminal peptidecrystal structure of alfalfa mosaic virus RNA 3'UTR in complex with coat protein N terminal peptide
Structural highlights
Function[CAPSD_AMVYS] Capsid protein. Binds to the to the 3' end of the nonpolyadenylated viral RNA and is involved in viral RNA translation initiation. Probably binds RNA and plays a role in packaging (By similarity). Publication Abstract from PubMedAlfalfa mosaic virus genomic RNAs are infectious only when the viral coat protein binds to the RNA 3' termini. The crystal structure of an alfalfa mosaic virus RNA-peptide complex reveals that conserved AUGC repeats and Pro-Thr-x-Arg-Ser-x-x-Tyr coat protein amino acids cofold upon interacting. Alternating AUGC residues have opposite orientation, and they base pair in different adjacent duplexes. Localized RNA backbone reversals stabilized by arginine-guanine interactions place the adenosines and guanines in reverse order in the duplex. The results suggest that a uniform, organized 3' conformation, similar to that found on viral RNAs with transfer RNA-like ends, may be essential for replication. Cofolding organizes alfalfa mosaic virus RNA and coat protein for replication.,Guogas LM, Filman DJ, Hogle JM, Gehrke L Science. 2004 Dec 17;306(5704):2108-11. PMID:15604410[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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