3GI1

Crystal Structure of the laminin-binding protein Lbp of Streptococcus pyogenes

Summary for 3GI1

• Entry DOI: 10.2210/pdb3gi1/pdb
• Descriptor: Laminin-binding protein of group A streptococci, ZINC ION (3 entities in total)
• Functional Keywords: zinc-binding receptor, metal-binding, helical backbone, alpha/beta domains, laminin-binding protein, lbp, transport, metal transport
• Biological source: Streptococcus pyogenes
• Total number of polymer chains: 2
• Total formula weight: 63950.96

Authors

Linke, C.,Caradoc-Davies, T.T.,Young, P.G.,Proft, T.,Baker, E.N. (deposition date: 2009-03-04, release date: 2009-08-04, Last modification date: 2023-11-01)

Primary citation

Linke, C.,Caradoc-Davies, T.T.,Young, P.G.,Proft, T.,Baker, E.N.
The laminin-binding protein Lbp from Streptococcus pyogenes is a zinc receptor
J.Bacteriol., 191:5814-5823, 2009

PubMed Abstract: The common pathogen Streptococcus pyogenes colonizes the human skin and tonsils and can invade underlying tissues. This requires the adhesion of S. pyogenes to host surface receptors mediated through adhesins. The laminin-binding protein Lbp has been suggested as an adhesin, specific for the human extracellular matrix protein laminin. Sequence alignments, however, indicate a relationship between Lbp and a family of bacterial metal-binding receptors. To further analyze the role of Lbp in S. pyogenes and its potential role in pathogenicity, Lbp has been crystallized, and its structure has been solved at a resolution of 2.45 A (R = 0.186; R(free) = 0.251). Lbp has the typical metal-binding receptor fold, comprising two globular (beta/alpha)(4) domains connected by a helical backbone. The two domains enclose the metal-binding site, which contains a zinc ion. The interaction of Lbp with laminin was further investigated and shown to be specific in vitro. Localization studies with antibodies specific for Lbp show that the protein is attached to the membrane. The data suggest that Lbp is primarily a zinc-binding protein, and we suggest that its interaction with laminin in vivo may be mediated via zinc bound to laminin.

PubMed: 19617361
DOI: 10.1128/JB.00485-09

Experimental method

X-RAY DIFFRACTION (2.45 Å)