2J44
Alpha-glucan binding by a streptococcal virulence factor
Summary for 2J44
Entry DOI | 10.2210/pdb2j44/pdb |
Related PRD ID | PRD_900009 PRD_900010 |
Descriptor | ALKALINE AMYLOPULLULANASE, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (5 entities in total) |
Functional Keywords | virulence, pullulanase, glycogen binding, streptococcus pneumoniae, carbohydrate-binding module |
Biological source | STREPTOCOCCUS PNEUMONIAE |
Cellular location | Secreted, cell wall; Peptidoglycan-anchor (By similarity): Q97SQ7 |
Total number of polymer chains | 1 |
Total formula weight | 26719.33 |
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: 2023-12-13) |
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 Cited by 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: 17187076DOI: 10.1038/NSMB1187 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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