TY - JOUR
T1 - Crystal structure of ATVORF273, a new fold for a thermo- and acido-stable protein from the Acidianus two-tailed virus
AU - Felisberto-Rodrigues, Catarina
AU - Blangy, Stéphanie
AU - Goulet, Adeline
AU - Vestergaard, Gisle Alberg
AU - Cambillau, Christian
AU - Garrett, Roger Antony
AU - Ortiz-Lombardía, Miguel
N1 - e45847
PY - 2012/10/8
Y1 - 2012/10/8
N2 - Acidianus two-tailed virus (ATV) infects crenarchaea of the genus Acidianus living in terrestrial thermal springs at extremely high temperatures and low pH. ATV is a member of the Bicaudaviridae virus family and undergoes extra-cellular development of two tails, a process that is unique in the viral world. To understand this intriguing phenomenon, we have undertaken structural studies of ATV virion proteins and here we present the crystal structure of one of these proteins, ATVORF273. ATVORF273 forms tetramers in solution and a molecular envelope is provided for the tetramer, computed from small-angle X-ray scattering (SAXS) data. The crystal structure has properties typical of hyperthermostable proteins, including a relatively high number of salt bridges. However, the protein also exhibits flexible loops and surface pockets. Remarkably, ATVORF273 displays a new α + β protein fold, consistent with the absence of homologues of this protein in public sequence databases.
AB - Acidianus two-tailed virus (ATV) infects crenarchaea of the genus Acidianus living in terrestrial thermal springs at extremely high temperatures and low pH. ATV is a member of the Bicaudaviridae virus family and undergoes extra-cellular development of two tails, a process that is unique in the viral world. To understand this intriguing phenomenon, we have undertaken structural studies of ATV virion proteins and here we present the crystal structure of one of these proteins, ATVORF273. ATVORF273 forms tetramers in solution and a molecular envelope is provided for the tetramer, computed from small-angle X-ray scattering (SAXS) data. The crystal structure has properties typical of hyperthermostable proteins, including a relatively high number of salt bridges. However, the protein also exhibits flexible loops and surface pockets. Remarkably, ATVORF273 displays a new α + β protein fold, consistent with the absence of homologues of this protein in public sequence databases.
U2 - 10.1371/journal.pone.0045847
DO - 10.1371/journal.pone.0045847
M3 - Journal article
C2 - 23056221
SN - 1932-6203
VL - 7
JO - PLoS Computational Biology
JF - PLoS Computational Biology
IS - 10
ER -