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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 1(67), p. 169-172

DOI: 10.1107/s1744309110050785

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The mimivirus R355 gene product: preliminary crystallographic analysis of a putative ubiquitin-like protein-specific protease

Journal article published in 2010 by Sandra Jeudy, Audrey Lartigue, Pascal Mansuelle ORCID, Yuki Ogata, Chantal Abergel
This paper is available in a repository.
This paper is available in a repository.

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Abstract

The complete genome sequence of the largest known double-stranded DNA virus, mimivirus, reveals the presence of a gene (denoted R355) that potentially encodes a cysteine protease that is expressed late (after 6 h) in the infectious cycle of the virus. In order to verify a sequence-based functional prediction and understand its role during the infectious process, the R355 protein was produced to assay its proteolytic activity and solve its three-dimensional structure. Here, the preliminary crystallographic analysis of the recombinant viral protein is reported. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with a monomer in the asymmetric unit. A MAD data set was used for preliminary phasing using the selenium signal from a selenomethionine-substituted protein crystal.