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

J 2007

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

PLEVKA, Pavel, Kaspars TARS, Andris ZELTINS, Ina BALKE, Erkki TRUVE et. al.

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

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

Změněno: 30. 3. 2017 11:28, Mgr. Eva Špillingová

Anotace

V originále

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.

Citovat

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.

@article{1376898,
   author = {Plevka, Pavel and Tars, Kaspars and Zeltins, Andris and Balke, Ina and Truve, Erkki and Liljas, Lars},
   article_location = {USA},
   article_number = {2},
   doi = {http://dx.doi.org/10.1016/j.virol.2007.07.028},
   keywords = {Ryegrass mottle virus; sobemovirus; virus structure; virus assembly},
   language = {eng},
   issn = {0042-6822},
   journal = {Virology},
   title = {The three-dimensional structure of ryegrass mottle virus at 2.9 angstrom resolution},
   volume = {369},
   year = {2007}
}

TY  - JOUR
ID  - 1376898
AU  - Plevka, Pavel - Tars, Kaspars - Zeltins, Andris - Balke, Ina - Truve, Erkki - Liljas, Lars
PY  - 2007
TI  - The three-dimensional structure of ryegrass mottle virus at 2.9 angstrom resolution
JF  - Virology
VL  - 369
IS  - 2
SP  - 364-374
EP  - 364-374
PB  - Academic Press
SN  - 00426822
KW  - Ryegrass mottle virus
KW  - sobemovirus
KW  - virus structure
KW  - virus assembly
N2  - 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.
ER  -

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. \textit{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.

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