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PDBsum entry 2j1v

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protein ligands metals Protein-protein interface(s) links
Carbohydrate-binding protein PDB id
2j1v

 

 

 

 

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Contents
Protein chains
142 a.a. *
Ligands
NAG-GAL-FUC
Metals
_CA ×2
Waters ×624
* Residue conservation analysis
PDB id:
2j1v
Name: Carbohydrate-binding protein
Title: Structure of a streptococcus pneumoniae fucose binding module in complex with the blood group h-trisaccharide
Structure: Fucolectin-related protein. Chain: a, b. Fragment: fucose binding module, residues 601-745. Synonym: fucose binding module. Engineered: yes
Source: Streptococcus pneumoniae. Organism_taxid: 170187. Strain: tigr4. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.45Å     R-factor:   0.154     R-free:   0.208
Authors: A.B.Boraston,D.Wang,R.D.Burke
Key ref:
A.B.Boraston et al. (2006). Blood group antigen recognition by a Streptococcus pneumoniae virulence factor. J Biol Chem, 281, 35263-35271. PubMed id: 16987809 DOI: 10.1074/jbc.M607620200
Date:
15-Aug-06     Release date:   06-Sep-06    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
A0A0H2US34  (A0A0H2US34_STRPN) -  Fucolectin-related protein from Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1038 a.a.
142 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
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 (0.39, 0.48, 0.23, and 0.28 electrons/Å^3) for the fucose, type II blood group H-trisaccharide, blood group A-tetrasaccharide analogue, and Lewis^y antigen complexes, respectively. Relevant residues involved in binding are shown in gray stick representation and labeled.
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
19908036 D.Guillén, S.Sánchez, and R.Rodríguez-Sanoja (2010).
Carbohydrate-binding domains: multiplicity of biological roles.
  Appl Microbiol Biotechnol, 85, 1241-1249.  
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
19422833 E.Ficko-Blean, and A.B.Boraston (2009).
N-acetylglucosamine recognition by a family 32 carbohydrate-binding module from Clostridium perfringens NagH.
  J Mol Biol, 390, 208-220.
PDB codes: 2w1q 2w1s 2w1u 2wdb
  19194003 K.J.Gregg, and A.B.Boraston (2009).
Cloning, recombinant production, crystallization and preliminary X-ray diffraction analysis of a family 101 glycoside hydrolase from Streptococcus pneumoniae.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 133-135.  
19608744 M.A.Higgins, G.E.Whitworth, N.El Warry, M.Randriantsoa, E.Samain, R.D.Burke, D.J.Vocadlo, and A.B.Boraston (2009).
Differential recognition and hydrolysis of host carbohydrate antigens by Streptococcus pneumoniae family 98 glycoside hydrolases.
  J Biol Chem, 284, 26161-26173.
PDB codes: 2wmf 2wmg 2wmh 2wmi 2wmj 2wmk
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.
PDB codes: 2vm9 2vmc 2vmd 2vme
18508271 S.A.Shelburne, M.T.Davenport, D.B.Keith, and J.M.Musser (2008).
The role of complex carbohydrate catabolism in the pathogenesis of invasive streptococci.
  Trends Microbiol, 16, 318-325.  
18553932 S.Farrand, E.Hotze, P.Friese, S.K.Hollingshead, D.F.Smith, R.D.Cummings, G.L.Dale, and R.K.Tweten (2008).
Characterization of a streptococcal cholesterol-dependent cytolysin with a lewis y and b specific lectin domain.
  Biochemistry, 47, 7097-7107.  
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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