1m1c | pdb_00001m1c
Structure of the L-A virus
Structural highlights
Function[GAG_SCVLA] Capsid protein self-assembles to form an icosahedral capsid with a T=2 symmetry, 40 nm in diameter, and consisting of 60 capsid proteins asymmetric dimers. The capsid encapsulates the genomic dsRNA and the polymerase and remains intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nacent transcripts are transcribed within the structural confines of the virion and are extruded into the cytoplasm.[1] [2] Binds and removes 5' cap structures from cellular mRNA. Forms a covalent bond with m7GMP through His-154 of the capsid protein while releasing the mRNA body.[3] [4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of the yeast L-A virus was determined by X-ray crystallography at 3.4 A resolution. The L-A dsRNA virus is 400 A in diameter and contains a single protein shell of 60 asymmetric dimers of the coat protein, a feature common among the inner protein shells of dsRNA viruses and probably related to their unique mode of transcription and replication. The two identical subunits in each dimer are in non-equivalent environments and show substantially different conformations in specific surface regions. The L-A virus decaps cellular mRNA to efficiently translate its own uncapped mRNA. Our structure reveals a trench at the active site of the decapping reaction and suggests a role for nearby residues in the reaction. L-A virus at 3.4 A resolution reveals particle architecture and mRNA decapping mechanism.,Naitow H, Tang J, Canady M, Wickner RB, Johnson JE Nat Struct Biol. 2002 Oct;9(10):725-8. PMID:12244300[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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