Metal binding is critical for the folding and function of laminin binding protein, Lmb of Streptococcus agalactiae.

ABSTRACT: Lmb is a 34 kDa laminin binding surface adhesin of Streptococcus agalactiae. The structure of Lmb reported by us recently has shown that it consists of a metal binding crevice, in which a zinc ion is coordinated to three highly conserved histidines. To elucidate the structural and functional significance of the metal ion in Lmb, these histidines have been mutated to alanine and single, double and triple mutants were generated. These mutations resulted in insolubility of the protein and revealed altered secondary and tertiary structures, as evidenced by circular dichroism and fluorescence spectroscopy studies. The mutations also significantly decreased the binding affinity of Lmb to laminin, implicating the role played by the metal binding residues in maintaining the correct conformation of

SUBMITTER: Ragunathan P 

PROVIDER: S-EPMC3691195 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature