Structural basis for the recognition of sulfur in phosphorothioated DNA.

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 S¹⁸⁷RGRR¹⁹¹ loop inserts into the DNA major groove to make contacts with the bases of the G_PSGCC core sequence. Mutating key residues of SBD impairs PT-DNA association. More than 1000 sequenced microbial species from fourteen phyla contain

SUBMITTER: Liu G 

PROVIDER: S-EPMC6224610 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature