Structural and Functional Analysis of the Tandem ß-Zipper Interaction of a Streptococcal Protein with Human Fibronectin

TY - JOUR

T1 - Structural and Functional Analysis of the Tandem ß-Zipper Interaction of a Streptococcal Protein with Human Fibronectin

AU - Norris, Nicole C

AU - Bingham, Richard J

AU - Harris, Gemma

AU - Speakman, Adrian

AU - Jones, Richard P O

AU - Leech, Andrew

AU - Turkenburg, Johan P

AU - Potts, Jennifer R

PY - 2011/11/4

Y1 - 2011/11/4

N2 - Bacterial fibronectin-binding proteins (FnBPs) contain a large intrinsically disordered region (IDR) that mediates adhesion of bacteria to host tissues, and invasion of host cells, through binding to fibronectin (Fn). These FnBP IDRs consist of Fn-binding repeats (FnBRs) that form a highly extended tandem ß-zipper interaction on binding to the N-terminal domain of Fn. Several FnBR residues are highly conserved across bacterial species, and here we investigate their contribution to the interaction. Mutation of these residues to alanine in SfbI-5 (a disordered FnBR from the human pathogen Streptococcus pyogenes) reduced binding, but for each residue the change in free energy of binding was

AB - Bacterial fibronectin-binding proteins (FnBPs) contain a large intrinsically disordered region (IDR) that mediates adhesion of bacteria to host tissues, and invasion of host cells, through binding to fibronectin (Fn). These FnBP IDRs consist of Fn-binding repeats (FnBRs) that form a highly extended tandem ß-zipper interaction on binding to the N-terminal domain of Fn. Several FnBR residues are highly conserved across bacterial species, and here we investigate their contribution to the interaction. Mutation of these residues to alanine in SfbI-5 (a disordered FnBR from the human pathogen Streptococcus pyogenes) reduced binding, but for each residue the change in free energy of binding was

UR - http://www.scopus.com/inward/record.url?scp=80055073240&partnerID=8YFLogxK

U2 - 10.1074/jbc.M111.276592

DO - 10.1074/jbc.M111.276592

M3 - Article

C2 - 21840989

SN - 0021-9258

VL - 286

SP - 38311

EP - 38320

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 44

ER -