The three-dimensional structure of ryegrass mottle virus at 2.9 angstrom resolution

PLEVKA, Pavel, Kaspars TARS, Andris ZELTINS, Ina BALKE, Erkki TRUVE a Lars LILJAS. The three-dimensional structure of ryegrass mottle virus at 2.9 angstrom resolution. Virology. USA: Academic Press, 2007, roč. 369, č. 2, s. 364-374. ISSN 0042-6822. Dostupné z: https://dx.doi.org/10.1016/j.virol.2007.07.028.

Základní údaje

• Originální název: The three-dimensional structure of ryegrass mottle virus at 2.9 angstrom resolution
• Autoři: PLEVKA, Pavel, Kaspars TARS, Andris ZELTINS, Ina BALKE, Erkki TRUVE a Lars LILJAS.
• Vydání: Virology, USA, Academic Press, 2007, 0042-6822.

Další údaje

• Originální jazyk: angličtina
• Typ výsledku: Článek v odborném periodiku
• Obor: 10600 1.6 Biological sciences
• Stát vydavatele: Spojené státy
• Utajení: není předmětem státního či obchodního tajemství
• Impakt faktor: Impact factor: 3.765
• Organizační jednotka: Středoevropský technologický institut
• Doi: http://dx.doi.org/10.1016/j.virol.2007.07.028
• UT WoS: 000251263200013
• Klíčová slova anglicky: Ryegrass mottle virus; sobemovirus; virus structure; virus assembly
• Štítky: neMU

Anotace

The cystal structure of the sobemovirus Ryegrass mottle virus (RGMoV) has been determined at 2.9 angstrom resolution. The coat protein has a canonical jellyroll beta-sandwich fold. In comparison to other sobemoviruses the RGMoV coat protein is missing several residues in two of the loop regions. The first loop contributes to contacts between subunits around the quasi-threefold symmetry axis. The altered contact interface results in tilting of the subunits towards the quasi-threefold axis. The assembly of the T = 3 capsid of sobemoviruses is controlled by the N-termini of C subunits forming a so-called beta-annulus. The other loop that is smaller in the RGMoV structure contains a helix that participates in stabilization of the beta-annulus in other sobernoviruses. The loss of interaction between the RGMoV loop and the beta-annulus has been compensated for by additional interactions between the N-terminal arms. As a consequence of these differences, the diameter of the RGMoV particle is 8 A smaller than that of the other sobemoviruses. The interactions of coat proteins in sobemovirus capsids involve calciurn ions. Depletion of calcium ions results in particle swelling, which is considered a first step in disassembly. We could not identify any density for metal ions in the proximity of the conserved residues normally involved in calcium binding, but the RGMoV structure does not show any signs of swelling. A likely reason is the low pH (3.0) of the crystallization buffer in which the groups interacting with the calcium ions are not charged. (c) 2007 Elsevier Inc. All rights reserved.