1E57

PHYSALIS MOTTLE VIRUS: EMPTY CAPSID

1E57 の概要

• エントリーDOI: 10.2210/pdb1e57/pdb
• 関連するPDBエントリー: 1QJZ
• 分子名称: PHYSALIS MOTTLE VIRUS (1 entity in total)
• 機能のキーワード: virus, coat protein (viral), icosahedral virus
• 由来する生物種: PHYSALIS MOTTLE VIRUS
• 細胞内の位置: Virion : P36351
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 59969.77

構造登録者

Krishna, S.S.,Sastri, M.,Savithri, H.S.,Murthy, M.R.N. (登録日: 2000-07-18, 公開日: 2001-04-26, 最終更新日: 2023-12-13)

主引用文献

Krishna, S.S.,Sastri, M.,Savithri, H.S.,Murthy, M.R.N.
Structural Studies on the Empty Capsids of Physalis Mottle Virus
J.Mol.Biol., 307:1035-, 2001

PubMed Abstract: The three-dimensional crystal structure of the empty capsid of Physalis mottle tymovirus has been determined to 3.2 A resolution. The empty capsids crystallized in the space group P1, leading to 60-fold non-crystallographic redundancy. The known structure of Physalis mottle virus was used as a phasing model to initiate the structure determination by real-space electron-density averaging. The main differences between the structures of the native and the empty capsids were in residues 10 to 28 of the A-subunit, residues 1 to 9 of the B-subunit and residues 1 to 5 of the C-subunit, which are ordered only in the native virus particles. An analysis of the subunit disposition reveals that the virus has expanded radially outward by approximately 1.8 A in the empty particles. The A-subunits move in a direction that makes 10 degrees to the icosahedral 5-fold axes of symmetry. The B and C-subunits move along vectors making 12 degrees and 15 degrees to the quasi 6-fold axes. The quaternary organization of the pentameric and hexameric capsomeres are not altered significantly. However, the pentamer-hexamer contacts are reduced. Therefore, encapsidation of RNA appears to cause a reduction in the particle radius concomittant with the ordering of the N-terminal arm in the three subunits. These structural changes in Physalis mottle virus appear to be larger than the corresponding changes observed in viruses for which both the empty and full particle structures have been determined.

PubMed: 11286554
DOI: 10.1006/JMBI.2001.4533

実験手法

X-RAY DIFFRACTION (3.2 Å)