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Structural basis for the recognition of sulfur in phosphorothioated DNA.
- Source :
- Nature Communications; 11/8/2018, Vol. 9 Issue 1, p1-1, 1p
- Publication Year :
- 2018
-
Abstract
- There have been very few reports on protein domains that specifically recognize sulfur. Here we present the crystal structure of the sulfur-binding domain (SBD) from the DNA phosphorothioation (PT)-dependent restriction endonuclease ScoMcrA. SBD contains a hydrophobic surface cavity that is formed by the aromatic ring of Y164, the pyrolidine ring of P165, and the non-polar side chains of four other residues that serve as lid, base, and wall of the cavity. The SBD and PT-DNA undergo conformational changes upon binding. The S<superscript>187</superscript>RGRR<superscript>191</superscript> loop inserts into the DNA major groove to make contacts with the bases of the G<subscript>PS</subscript>GCC core sequence. Mutating key residues of SBD impairs PT-DNA association. More than 1000 sequenced microbial species from fourteen phyla contain SBD homologs. We show that three of these homologs bind PT-DNA in vitro and restrict PT-DNA gene transfer in vivo. These results show that SBD-like PT-DNA readers exist widely in prokaryotes. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 20411723
- Volume :
- 9
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- Nature Communications
- Publication Type :
- Academic Journal
- Accession number :
- 132911840
- Full Text :
- https://doi.org/10.1038/s41467-018-07093-1