Crystal structure of ATV^ORF273, a new fold for a thermo- and acido-stable protein from the Acidianus two-tailed virus

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 - P L o S One

JF - P L o S One

IS - 10

ER -