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Crystal structure of a putative type I restriction-modification S subunit from Mycoplasma genitalium

AuthorsCalisto, Bárbara M. ; Pich, Oscar Q.; Piñol, Jaume; Fita, Ignacio ; Querol, Enrique; Carpena, Xavi
KeywordsCrystal structure
Type I restriction and modification system
Mycoplasma genitalium
DNA recognition
Issue Date26-Aug-2005
PublisherAcademic Press
CitationJournal of Molecular Biology 351(4): 749-762 (2005)
AbstractThe crystal structure of the eubacteria Mycoplasma genitalium ORF MG438 polypeptide, determined by multiple anomalous dispersion and refined at 2.3 Å resolution, reveals the organization of S subunits from the Type I restriction and modification system. The structure consists of two globular domains, with about 150 residues each, separated by a pair of 40 residue long antiparallel α-helices. The globular domains correspond to the variable target recognition domains (TRDs), as previously defined for S subunits on sequence analysis, while the two helices correspond to the central (CR1) and C-terminal (CR2) conserved regions, respectively. The structure of the MG438 subunit presents an overall cyclic topology with an intramolecular 2-fold axis that superimposes the N and the C-half parts, each half containing a globular domain and a conserved helix. TRDs are found to be structurally related with the small domain of the Type II N6-adenine DNA MTase TaqI. These relationships together with the structural peculiarities of MG438, in particular the presence of the intramolecular quasi-symmetry, allow the proposal of a model for S subunits recognition of their DNA targets in agreement with previous experimental results. In the crystal, two subunits of MG438 related by a crystallographic 2-fold axis present a large contact area mainly involving the symmetric interactions of a cluster of exposed hydrophobic residues. Comparison with the recently reported structure of an S subunit from the archaea Methanococcus jannaschii highlights the structural features preserved despite a sequence identity below 20%, but also reveals important differences in the globular domains and in their disposition with respect to the conserved regions.
Publisher version (URL)http://dx.doi.org/10.1016/j.jmb.2005.06.050
Identifiersdoi: 10.1016/j.jmb.2005.06.050
issn: 0022-2836
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