Distinct single amino acid replacements in the control of virulence regulator protein differentially impact streptococcal pathogenesis.

ABSTRACT: Sequencing of invasive strains of group A streptococci (GAS) has revealed a diverse array of single nucleotide polymorphisms in the gene encoding the control of virulence regulator (CovR) protein. However, there is limited information regarding the molecular mechanisms by which CovR single amino acid replacements impact GAS pathogenesis. The crystal structure of the CovR C-terminal DNA-binding domain was determined to 1.50 Å resolution and revealed a three-stranded β-sheet followed by a winged helix-turn-helix DNA binding motif. Modeling of the CovR protein-DNA complex indicated that CovR single amino acid replacements observed in clinical GAS isolates could directly alter protein-DNA interaction and impact protein structure. Isoallelic GAS strains that varied by a single amino acid replac

SUBMITTER: Horstmann N 

PROVIDER: S-EPMC3197619 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature