2j22 | pdb_00002j22

Structure of a Streptococcus pneumoniae fucose binding module, SpX-3

spinqualitylabelsall models 2j22, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2j22 is a 1 chain structure with sequence from Streptococcus pneumoniae TIGR4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: CA, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2US34_STRPN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The Streptococcus pneumoniae fucose utilization operon includes a gene encoding a virulence factor that belongs to family 98 in the glycoside hydrolase classification. This protein contains a C-terminal triplet of fucose binding modules that have significant amino acid sequence identity with the Anguilla anguilla fucolectin. Functional studies of these fucose binding modules reveal binding to fucosylated oligosaccharides and suggest the importance of multivalent binding. The high resolution crystal structures of ligand bound forms of one fucose binding module uncovers the molecular basis of fucose, ABH blood group antigen, and Lewisy antigen binding. These studies are extended by fluorescence microscopy to show specific binding to mouse lung tissue. These modules define a new family of carbohydrate binding modules now classified as family 47. Blood group antigen recognition by a Streptococcus pneumoniae virulence factor.,Boraston AB, Wang D, Burke RD J Biol Chem. 2006 Nov 17;281(46):35263-71. Epub 2006 Sep 20. PMID:16987809 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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