Defining the metal specificity of a multifunctional biofilm adhesion protein.

ABSTRACT: The accumulation associated protein (Aap) of Staphylococcus epidermidis mediates intercellular adhesion events necessary for biofilm growth. This process depends upon Zn²⁺ -induced self-assembly of G5 domains within the B-repeat region of the protein, forming anti-parallel, intertwined protein "ropes" between cells. Pleomorphism in the Zn²⁺ -coordinating residues was observed in previously solved crystal structures, suggesting that the metal binding site might accommodate other transition metals and thereby support dimerization. By use of carefully selected buffer systems and a specialized approach to analyze sedimentation velocity analytical ultracentrifugation data, we were able to analyze low-affinity metal binding events in solution. Our data show that both Zn

SUBMITTER: Chaton CT 

PROVIDER: S-EPMC5606542 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature