1M1C
Structure of the L-A virus
Summary for 1M1C
Entry DOI | 10.2210/pdb1m1c/pdb |
Descriptor | Major coat protein (1 entity in total) |
Functional Keywords | dsrna virus structure; rna-protein interaction; mrna decapping; l-a virus; quai-equivalence, icosahedral virus, virus |
Biological source | Saccharomyces cerevisiae virus L-A (L1) |
Cellular location | Virion (Potential): P32503 |
Total number of polymer chains | 2 |
Total formula weight | 152140.06 |
Authors | Naitow, H.,Tang, J.,Canady, M.,Wickner, R.B.,Johnson, J.E. (deposition date: 2002-06-18, release date: 2002-10-02, Last modification date: 2024-02-14) |
Primary citation | Naitow, H.,Tang, J.,Canady, M.,Wickner, R.B.,Johnson, J.E. L-A virus at 3.4 A resolution reveals particle architecture and mRNA decapping mechanism. Nat.Struct.Biol., 9:725-728, 2002 Cited by PubMed Abstract: The 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. PubMed: 12244300DOI: 10.1038/nsb844 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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