PDBsum entry 1k12

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Sugar binding protein PDB id
Protein chain
158 a.a. *
Waters ×130
* Residue conservation analysis
PDB id:
Name: Sugar binding protein
Title: Fucose binding lectin
Structure: Lectin. Chain: a
Source: Anguilla anguilla. European eel. Organism_taxid: 7936
Biol. unit: Hexamer (from PQS)
1.90Å     R-factor:   0.190     R-free:   0.239
Authors: M.A.Bianchet,E.W.Odom,G.R.Vasta,L.M.Amzel
Key ref:
M.A.Bianchet et al. (2002). A novel fucose recognition fold involved in innate immunity. Nat Struct Biol, 9, 628-634. PubMed id: 12091873 DOI: 10.1038/nsb817
23-Sep-01     Release date:   31-Jul-02    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q7SIC1  (FUCL_ANGAN) -  Fucolectin
158 a.a.
158 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     cell adhesion   4 terms 
  Biochemical function     carbohydrate binding     4 terms  


DOI no: 10.1038/nsb817 Nat Struct Biol 9:628-634 (2002)
PubMed id: 12091873  
A novel fucose recognition fold involved in innate immunity.
M.A.Bianchet, E.W.Odom, G.R.Vasta, L.M.Amzel.
Anguilla anguilla agglutinin (AAA), a fucolectin found in the serum of European eel, participates in the recognition of bacterial liposaccharides by the animal innate immunity system. Because AAA specifically recognizes fucosylated terminals of H and Lewis (a) blood groups, it has been used extensively as a reagent in blood typing and histochemistry. AAA contains a newly discovered carbohydrate recognition domain present in proteins of organisms ranging from bacteria to vertebrates. The crystal structure of the complex of AAA with alpha-L-fucose characterizes the novel fold of this entire lectin family, identifying the residues that provide the structural determinants of oligosaccharide specificity. Modification of these residues explains how the different isoforms in serum can provide a diverse pathogen-specific recognition.
  Selected figure(s)  
Figure 3.
Figure 3. Schematic representation of protein interactions with ligands. a, Interactions observed in the complex. b, Interactions predicted between a D-galactose derivate and AAA.
Figure 4.
Figure 4. Model of the interactions between AAA and a terminal fucosyl trisaccharide. a, Le^a antigen. b, H-type 1. Residues and trisaccharides are shown using the same representation and color scheme of Fig. 1, with the exception of the carbon atoms (pink) of the ligand.
  The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2002, 9, 628-634) copyright 2002.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20812023 P.Popovics, and A.J.Stewart (2011).
GPR39: a Zn(2+)-activated G protein-coupled receptor that regulates pancreatic, gastrointestinal and neuronal functions.
  Cell Mol Life Sci, 68, 85-95.  
20615601 A.Cooper, and M.W.Kennedy (2010).
Biofoams and natural protein surfactants.
  Biophys Chem, 151, 96.  
20152053 A.Konno, S.Yonemaru, A.Kitagawa, K.Muramoto, T.Shirai, and T.Ogawa (2010).
Protein engineering of conger eel galectins by tracing of molecular evolution using probable ancestral mutants.
  BMC Evol Biol, 10, 43.  
20596876 M.G.Parisi, M.Cammarata, G.Benenati, G.Salerno, V.Mangano, A.Vizzini, and N.Parrinello (2010).
A serum fucose-binding lectin (DlFBL) from adult Dicentrarchus labrax is expressed in larva and juvenile tissues and contained in eggs.
  Cell Tissue Res, 341, 279-288.  
20152153 O.Sulák, G.Cioci, M.Delia, M.Lahmann, A.Varrot, A.Imberty, and M.Wimmerová (2010).
A TNF-like trimeric lectin domain from Burkholderia cenocepacia with specificity for fucosylated human histo-blood group antigens.
  Structure, 18, 59-72.
PDB code: 2wq4
20939100 S.Kalkhof, S.Haehn, M.Paulsson, N.Smyth, J.Meiler, and A.Sinz (2010).
Computational modeling of laminin N-terminal domains using sparse distance constraints from disulfide bonds and chemical cross-linking.
  Proteins, 78, 3409-3427.  
19324764 R.I.Fleming, C.D.Mackenzie, A.Cooper, and M.W.Kennedy (2009).
Foam nest components of the tungara frog: a cocktail of proteins conferring physical and biological resilience.
  Proc Biol Sci, 276, 1787-1795.  
18484336 F.J.Stevens (2008).
Possible evolutionary links between immunoglobulin light chains and other proteins involved in amyloidosis.
  Amyloid, 15, 96.  
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.  
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.  
17703188 O.Ichikawa, M.Osawa, N.Nishida, N.Goshima, N.Nomura, and I.Shimada (2007).
Structural basis of the collagen-binding mode of discoidin domain receptor 2.
  EMBO J, 26, 4168-4176.
PDB code: 2z4f
16987809 A.B.Boraston, D.Wang, and R.D.Burke (2006).
Blood group antigen recognition by a Streptococcus pneumoniae virulence factor.
  J Biol Chem, 281, 35263-35271.
PDB codes: 2j1r 2j1s 2j1t 2j1u 2j1v 2j22
16990278 E.Ficko-Blean, and A.B.Boraston (2006).
The interaction of a carbohydrate-binding module from a Clostridium perfringens N-acetyl-beta-hexosaminidase with its carbohydrate receptor.
  J Biol Chem, 281, 37748-37757.
PDB codes: 2j1a 2j1e 2j1f 2j7m
16251191 E.W.Odom, and G.R.Vasta (2006).
Characterization of a binary tandem domain F-type lectin from striped bass (Morone saxatilis).
  J Biol Chem, 281, 1698-1713.  
  16820693 F.B.Moreno, D.E.Martil, B.S.Cavada, and Azevedo (2006).
Crystallization and preliminary X-ray diffraction analysis of an anti-H(O) lectin from Lotus tetragonolobus seeds.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 680-683.  
16704980 J.F.Sanchez, J.Lescar, V.Chazalet, A.Audfray, J.Gagnon, R.Alvarez, C.Breton, A.Imberty, and E.P.Mitchell (2006).
Biochemical and structural analysis of Helix pomatia agglutinin. A hexameric lectin with a novel fold.
  J Biol Chem, 281, 20171-20180.
PDB codes: 2ccv 2ce6
16436117 M.E.Nielsen, and M.D.Esteve-Gassent (2006).
The eel immune system: present knowledge and the need for research.
  J Fish Dis, 29, 65-78.  
15741346 J.Song, R.C.Tyler, R.L.Wrobel, R.O.Frederick, F.C.Vojtek, W.B.Jeon, M.S.Lee, and J.L.Markley (2005).
Solution structure of At3g04780.1-des15, an Arabidopsis thaliana ortholog of the C-terminal domain of human thioredoxin-like protein.
  Protein Sci, 14, 1059-1063.
PDB code: 1xoy
16239725 S.L.Newstead, J.N.Watson, A.J.Bennet, and G.Taylor (2005).
Galactose recognition by the carbohydrate-binding module of a bacterial sialidase.
  Acta Crystallogr D Biol Crystallogr, 61, 1483-1491.
PDB codes: 2bq9 2bzd
15292273 A.Miyanaga, T.Koseki, H.Matsuzawa, T.Wakagi, H.Shoun, and S.Fushinobu (2004).
Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose.
  J Biol Chem, 279, 44907-44914.
PDB codes: 1wd3 1wd4
15465324 G.R.Vasta, H.Ahmed, and E.W.Odom (2004).
Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates.
  Curr Opin Struct Biol, 14, 617-630.  
14997549 I.Hudáky, Z.Gáspári, O.Carugo, M.Cemazar, S.Pongor, and A.Perczel (2004).
Vicinal disulfide bridge conformers by experimental methods and by ab initio and DFT molecular computations.
  Proteins, 55, 152-168.  
12732625 M.Wimmerova, E.Mitchell, J.F.Sanchez, C.Gautier, and A.Imberty (2003).
Crystal structure of fungal lectin: six-bladed beta-propeller fold and novel fucose recognition mode for Aleuria aurantia lectin.
  J Biol Chem, 278, 27059-27067.
PDB code: 1ofz
12415289 E.Mitchell, C.Houles, D.Sudakevitz, M.Wimmerova, C.Gautier, S.Pérez, A.M.Wu, N.Gilboa-Garber, and A.Imberty (2002).
Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients.
  Nat Struct Biol, 9, 918-921.
PDB code: 1gzt
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 code is shown on the right.