Structural highlights
2j1t is a 2 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.
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| Method: | X-ray diffraction, Resolution 1.6Å |
| Ligands: | , , , , |
| 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boraston AB, Wang D, Burke RD. Blood group antigen recognition by a Streptococcus pneumoniae virulence factor. J Biol Chem. 2006 Nov 17;281(46):35263-71. Epub 2006 Sep 20. PMID:16987809 doi:10.1074/jbc.M607620200
