1msc | pdb_00001msc

CRYSTAL STRUCTURE OF MS2 COAT PROTEIN DIMER

spinqualitylabelsall models 1msc, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1msc is a 1 chain structure with sequence from Enterobacterio phage ms2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: MS2 COAT GENE (Enterobacterio phage MS2) Resources: FirstGlance, OCA, RCSB, PDBsum Function [COAT_BPMS2] Forms the phage shell; binds to the phage RNA. 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 PubMed BACKGROUND: The coat protein in RNA bacteriophages binds and encapsidates viral RNA, and also acts as translational repressor of viral replicase by binding to an RNA hairpin in the RNA genome. Because of its dual function, the MS2 coat protein is an interesting candidate for structural studies of protein-RNA interactions and protein-protein interactions. In this study, unassembled MS2 coat protein dimers were selected to analyze repressor activity and virus assembly. RESULTS: The crystal structure of a mutant MS2 coat protein that is defective in viral assembly yet retains repressor activity has been determined at 2.0 A resolution. The unassembled dimer is stabilized by interdigitation of alpha-helices, and the formation of a 10-stranded antiparallel beta-sheet across the interface between monomers. The substitution of arginine for tryptophan at residue 82 results in the formation of two new inter-subunit hydrogen bonds that further stabilize the dimer. Residues that influence RNA recognition, identified by molecular genetics, were located across the beta-sheet. Two of these residues (Tyr85 and Asn87) are displaced in the unliganded dimer and are located in the same beta-strand as the Trp-->Arg mutation. CONCLUSIONS: When compared with the structure of the coat protein in the assembled virus, differences in orientation of residues 85 and 87 suggest conformational adjustment on binding RNA in the first step of viral assembly. The substitution at residue 82 may affect virus assembly by imposing conformational restriction on the loop that makes critical inter-subunit contacts in the capsid. Crystal structure of the MS2 coat protein dimer: implications for RNA binding and virus assembly.,Ni CZ, Syed R, Kodandapani R, Wickersham J, Peabody DS, Ely KR Structure. 1995 Mar 15;3(3):255-63. PMID:7788292 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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