Open AccessThe mimivirus R355 gene product: preliminary crystallographic analysis of a putative ubiquitin‐like protein‐specific protease
Author(s) -
Jeudy Sandra,
Lartigue Audrey,
Mansuelle Pascal,
Ogata Yuki,
Abergel Chantal
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110050785
Subject(s) - recombinant dna , gene , orthorhombic crystal system , capsid , biology , cysteine protease , dna , virus , protease , virology , microbiology and biotechnology , chemistry , crystal structure , genetics , crystallography , biochemistry , enzyme
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 P 2 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.