ArticlePloS one2012
Crystal structure of ATV(ORF273), a new fold for a thermo- and acido-stable protein from the Acidianus two-tailed virus.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- ICTV Virus Taxonomy Profile: Bicaudaviridae.The Journal of general virology · 2018Article
- Viruses of archaea: Structural, functional, environmental and evolutionary genomics.Virus research · 2018Review
- Unification of the globally distributed spindle-shaped viruses of the Archaea.Journal of virology · 2014Article
- A survey of protein structures from archaeal viruses.Life (Basel, Switzerland) · 2013Review
- Archaeal viruses, not archaeal phages: an archaeological dig.Archaea (Vancouver, B.C.) · 2013Review
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
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, ATV(ORF273). ATV(ORF273) 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, ATV(ORF273) displays a new α + β protein fold, consistent with the absence of homologues of this protein in public sequence databases.
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