STRUCTURE OF SATELLITE TOBACCO NECROSIS VIRUS AT 3.0 A RESOLUTION
STRUCTURE OF SATELLITE TOBACCO NECROSIS VIRUS AT 3.0 A RESOLUTION
复制标题
DOI:
10.1016/0022-2836(82)90033-x
复制
发表时间:
1982-01-01
影响因子:
5.6
通讯作者:
STRANDBERG, B
中科院分区:
文献类型:
--
作者:
LILJAS, L;UNGE, T;STRANDBERG, B
The structure of satellite tobacco necrosis virus (STNV) was determined to 3.0 .ANG. resolution by X-ray crystallography. Electron density maps were obtained with phases based on 1 heavy-atom derivative and several cycles of phase refinement using the 60-fold non-crystallographic symmetry in the particle. A model for 1 protein subunit was built using a computer graphics display. The subunit is constructed mainly of a .beta.-roll structure forming 2 .beta.-sheets, each of 4 antiparallel strands. The N-termini of the subunits form bundles of 3 .alpha.-helices extending into the RNA region of the virus at the 3-fold axis. The topology of the polypeptide chain is the same as, and the conformation clearly similar to, that of the shell domains of the tomato bushy stunt virus (TBSV) and Southern bean mosaic virus (SBMV) protein subunits. The subunit packing in the T = 1 STNV structure is, however, significantly different from the packing of these T = 3 viruses: parts of some of the structural elements facing the RNA in TBSV and SBMV are utilized for subunit-subunit contacts in STNV. No RNA stucture is obvious in the present icosahedrally averaged electron density maps. The protein surface facing the RNA contains mainly hydrophilic residues, especially lysine and arginine.