Open AccessPreliminary crystallographic analysis of a polyadenylate synthase from Megavirus
Author(s) -
Lartigue Audrey,
Jeudy Sandra,
Bertaux Lionel,
Abergel Chantal
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112048257
Subject(s) - polyadenylation , escherichia coli , biology , palindrome , genome , gene , dna , atp synthase , microbiology and biotechnology , virology , enzyme , rna , genetics , biochemistry
Megavirus chilensis , a close relative of the Mimivirus giant virus, is also the most complex virus sequenced to date, with a 1.26 Mb double‐stranded DNA genome encoding 1120 genes. The two viruses share common regulatory elements such as a peculiar palindrome governing the termination/polyadenylation of viral transcripts. They also share a predicted polyadenylate synthase that presents a higher than average percentage of residue conservation. The Megavirus enzyme Mg561 was overexpressed in Escherichia coli , purified and crystallized. A 2.24 Å resolution MAD data set was recorded from a single crystal on the ID29 beamline at the ESRF.