4h0f

Mutant Structure of laminin-binding adhesin (Lmb) from Streptococcus agalactiae

spinqualitylabelsall models 4h0f, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4h0f is a 2 chain structure with sequence from Streptococcus agalactiae 2603V/R. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8DZ80_STRA5 Publication Abstract from PubMed 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 the protein for its binding to laminin. A highly disordered loop, proposed to be crucial for metal acquisition in homologous structures, was deleted in Lmb by mutation (DeltaLmb) and its crystal structure was solved at 2.6 A. The DeltaLmb structure was identical to the native Lmb structure with a bound zinc ion and exhibited laminin binding activity similar to wild type protein, suggesting that the loop might not have an important role in metal acquisition or adhesion in Lmb. Targeted mutations of histidine residues confirmed the importance of the zinc binding crevice for the structure and function of the Lmb adhesin. Metal binding is critical for the folding and function of laminin binding protein, Lmb of Streptococcus agalactiae.,Ragunathan P, Sridaran D, Weigel A, Shabayek S, Spellerberg B, Ponnuraj K PLoS One. 2013 Jun 24;8(6):e67517. doi: 10.1371/journal.pone.0067517. Print 2013. PMID:23826314 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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