2J43

Alpha-glucan recognition by family 41 carbohydrate-binding modules from streptococcal virulence factors

Summary for 2J43

• Entry DOI: 10.2210/pdb2j43/pdb
• Descriptor: SPYDX (2 entities in total)
• Functional Keywords: family 41, pullulanase, streptococcal, carbohydrate-binding module, glycogen binding, glycoside hydrolase
• Biological source: STREPTOCOCCUS PYOGENES
• Total number of polymer chains: 2
• Total formula weight: 50585.78

Authors

Lammerts van Bueren, A.,Higgins, M.,Wang, D.,Burke, R.D.,Boraston, A.B. (deposition date: 2006-08-24, release date: 2006-12-11, Last modification date: 2024-10-23)

Primary citation

Lammerts Van Bueren, A.,Higgins, M.,Wang, D.,Burke, R.D.,Boraston, A.B.
Identification and Structural Basis of Binding to Host Lung Glycogen by Streptococcal Virulence Factors.
Nat.Struct.Mol.Biol., 14:76-, 2007

PubMed Abstract: The ability of pathogenic bacteria to recognize host glycans is often essential to their virulence. Here we report structure-function studies of previously uncharacterized glycogen-binding modules in the surface-anchored pullulanases from Streptococcus pneumoniae (SpuA) and Streptococcus pyogenes (PulA). Multivalent binding to glycogen leads to a strong interaction with alveolar type II cells in mouse lung tissue. X-ray crystal structures of the binding modules reveal a novel fusion of tandem modules into single, bivalent functional domains. In addition to indicating a structural basis for multivalent attachment, the structure of the SpuA modules in complex with carbohydrate provides insight into the molecular basis for glycogen specificity. This report provides the first evidence that intracellular lung glycogen may be a novel target of pathogenic streptococci and thus provides a rationale for the identification of the streptococcal alpha-glucan-metabolizing machinery as virulence factors.

PubMed: 17187076
DOI: 10.1038/NSMB1187

Experimental method

X-RAY DIFFRACTION (1.6 Å)