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142 a.a.
_CA
Key reference
DOI no: 10.1074/jbc.M607620200 J Biol Chem 281:35263-35271 (2006) PubMed id: 16987809
Blood group antigen recognition by a Streptococcus pneumoniae virulence factor. A.B.Boraston, D.Wang, R.D.Burke. ABSTRACT
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.
Selected figure(s)
Figure 5.
FIGURE 5. Binding site architectures and electron density of fucose (A), the type II H-trisaccharide (B), the blood group A-tetrasaccharide analogue (C), and the Lewis^y antigen (D) bound to SpX-1. Electron density maps are maximum-likelihood(17)/[A] (27) weighted 2F[obs] - F[calc] electron density maps contoured at 1
Figure 6.
FIGURE 6. Hydrogen bonding schematics of fucose (A), the type II H-trisaccharide (B), the blood group A-tetrasaccharide analogue (C), and the Lewis^y antigen (D) bound to SpX-1. Potential hydrogen bonds are shown as dotted lines. Waters are shown as gray spheres. Potential hydrogen bond distances were between 2.5 and 3.3 Å.The above figures are reprinted by permission from the ASBMB: J Biol Chem (2006, 281, 35263-35271) copyright 2006. Figures were selected by an automated process.
Literature references that cite this PDB file's key reference
PubMed id Reference
19218457 C.Montanier, A.L.van Bueren, C.Dumon, J.E.Flint, M.A.Correia, J.A.Prates, S.J.Firbank, R.J.Lewis, G.G.Grondin, M.G.Ghinet, T.M.Gloster, C.Herve, J.P.Knox, B.G.Talbot, J.P.Turkenburg, J.Kerovuo, R.Brzezinski, C.M.Fontes, G.J.Davies, A.B.Boraston, and H.J.Gilbert (2009).
Evidence that family 35 carbohydrate binding modules display conserved specificity but divergent function.Proc Natl Acad Sci U S A, 106, 3065-3070.
PDB codes: 2vzp 2vzq 2vzr 2w1w 2w3j 2w46 2w47 2w87
18268333 G.W.Moy, S.A.Springer, S.L.Adams, W.J.Swanson, and V.D.Vacquier (2008).
Extraordinary intraspecific diversity in oyster sperm bindin.Proc Natl Acad Sci U S A, 105, 1993-1998.
18292090 K.J.Gregg, R.Finn, D.W.Abbott, and A.B.Boraston (2008).
Divergent modes of glycan recognition by a new family of carbohydrate-binding modules.J Biol Chem, 283, 12604-12613.
PDB codes: 2vmg 2vmh 2vmi 2vng 2vno 2vnr
18384150 K.S.Aragão, M.Satre, A.Imberty, and A.Varrot (2008).
Structure determination of Discoidin II from Dictyostelium discoideum and carbohydrate binding properties of the lectin domain.Proteins, 73, 43-52. The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.
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