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Life 2013, 3(1), 118-130; doi:10.3390/life3010118

A Survey of Protein Structures from Archaeal Viruses

Received: 15 December 2012 / Revised: 18 January 2013 / Accepted: 21 January 2013 / Published: 24 January 2013
(This article belongs to the Special Issue Extremophiles and Extreme Environments)
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Viruses that infect the third domain of life, Archaea, are a newly emerging field of interest. To date, all characterized archaeal viruses infect archaea that thrive in extreme conditions, such as halophilic, hyperthermophilic, and methanogenic environments. Viruses in general, especially those replicating in extreme environments, contain highly mosaic genomes with open reading frames (ORFs) whose sequences are often dissimilar to all other known ORFs. It has been estimated that approximately 85% of virally encoded ORFs do not match known sequences in the nucleic acid databases, and this percentage is even higher for archaeal viruses (typically 90%–100%). This statistic suggests that either virus genomes represent a larger segment of sequence space and/or that viruses encode genes of novel fold and/or function. Because the overall three-dimensional fold of a protein evolves more slowly than its sequence, efforts have been geared toward structural characterization of proteins encoded by archaeal viruses in order to gain insight into their potential functions. In this short review, we provide multiple examples where structural characterization of archaeal viral proteins has indeed provided significant functional and evolutionary insight.
Keywords: archaeal virus; thermophile; structural homology; archaea archaeal virus; thermophile; structural homology; archaea
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Dellas, N.; Lawrence, C.M.; Young, M.J. A Survey of Protein Structures from Archaeal Viruses. Life 2013, 3, 118-130.

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