crystal structure of atvorf273, a new fold for a thermo- and acido-stable protein from the acidianus two-tailed virusatvorf273的晶体结构,一个新的热,acido-stable蛋白质的折叠acidianus双尾病毒.pdfVIP
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crystal structure of atvorf273, a new fold for a thermo- and acido-stable protein from the acidianus two-tailed virusatvorf273的晶体结构,一个新的热,acido-stable蛋白质的折叠acidianus双尾病毒
Crystal Structure of ATVORF273, a New Fold for a Thermo-
and Acido-Stable Protein from the Acidianus Two-Tailed
Virus
1 ´ 1 1¤ 2
Catarina Felisberto-Rodrigues , Stephanie Blangy , Adeline Goulet , Gisle Vestergaard ,
1 2 ´ 1
Christian Cambillau , Roger A. Garrett , Miguel Ortiz-Lombardıa *
´
1 CNRS, Aix-Marseille Universite, AFMB, UMR 7257, Campus de Luminy, Marseille, France, 2 Archaea Centre, Department of Biology, University of Copenhagen,
Copenhagen, Denmark
Abstract
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 a zb protein fold, consistent with the absence of homologues of this pro
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