Structure of tomato bushy stunt virus. V. Coat protein sequence determination and its structural implications.
We report the chemically determined sequence of most of the polypeptide chain of the coat protein of tomato bushy stunt virus. Peptide locations have been determined by comparison with the high-resolution electron density map from X-ray crystallographic analysis as well as by conventional chemical overlaps. Three small gaps remain in the 387-residue sequence. Positively charged side-chains are concentrated in the N-terminal part of the polypeptide (the R domain) as well as on inward-facing surfaces of the S domain. There is homology of S-domain sequences with structurally corresponding residues in southern bean mosaic virus.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002213:Capsid; D008958:Models, Molecular; D010446:Peptide Fragments / Q000032:analysis; D010942:Plant Viruses / Q000032:analysis*; D011487:Protein Conformation; D014961:X-Ray Diffraction
D000596:Amino Acids; D010446:Peptide Fragments