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PDBsum entry 1log

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protein ligands metals Protein-protein interface(s) links
Lectin PDB id
1log

 

 

 

 

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Contents
Protein chains
180 a.a. *
46 a.a. *
51 a.a. *
Ligands
NAG-BMA-MAN ×2
Metals
_MN ×2
_CA ×2
Waters ×338
* Residue conservation analysis
PDB id:
1log
Name: Lectin
Title: X-ray structure of a (alpha-man(1-3)beta-man(1-4)glcnac)-lectin complex at 2.1 angstroms resolution
Structure: Legume isolectin i (alpha chain). Chain: a, c. Legume isolectin i (beta chain). Chain: b, d
Source: Lathyrus ochrus. Yellow-flowered pea. Organism_taxid: 3858. Organ: seed. Organ: seed
Biol. unit: Tetramer (from PQS)
Resolution:
2.10Å     R-factor:   0.175    
Authors: Y.Bourne,C.Cambillau
Key ref: Y.Bourne et al. (1990). X-ray structure of a (alpha-Man(1-3)beta-Man(1-4)GlcNAc)-lectin complex at 2.1-A resolution. The role of water in sugar-lectin interaction. J Biol Chem, 265, 18161-18165. PubMed id: 2211692
Date:
27-Jan-94     Release date:   30-Apr-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04122  (LECB_LATOC) -  Lectin beta-1 and beta-2 chains from Lathyrus ochrus
Seq:
Struc:
181 a.a.
180 a.a.*
Protein chain
P12306  (LEC1_LATOC) -  Mannose/glucose-specific lectin alpha 1 chain from Lathyrus ochrus
Seq:
Struc:
53 a.a.
46 a.a.*
Protein chain
P12306  (LEC1_LATOC) -  Mannose/glucose-specific lectin alpha 1 chain from Lathyrus ochrus
Seq:
Struc:
53 a.a.
51 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
J Biol Chem 265:18161-18165 (1990)
PubMed id: 2211692  
 
 
X-ray structure of a (alpha-Man(1-3)beta-Man(1-4)GlcNAc)-lectin complex at 2.1-A resolution. The role of water in sugar-lectin interaction.
Y.Bourne, P.Rougé, C.Cambillau.
 
  ABSTRACT  
 
We describe herein the high resolution refined x-ray structure of a trisaccharide, which is a part of the N-acetyllactosamine type glycan found in the majority of the N-glycosyl-proteins, complexed to the isolectin I. According to the potentials used by Imberty et al. (Imburty, A., Gerber, S., Tran, V., and Pérez, S. (1990) Glycoconjugate J. 7, 27-54) the trisaccharide is in a low-energy state. Only one mannose moiety establishes direct hydrogen bonds with the lectin, as it is the case for monosaccharide-lectin complexes. The comparison of our trisaccharide with the one determined in solution by Warin et al. (Warin, V., Baert, F., Fouret, R., Strecker, G., Fournet, B., and Montreuil, J. (1979) Carbohydr. Res. 76, 11-22) shows that both adopt roughly the same conformation. The differences in these two sugar structures allow us to assign the role of water molecules present in the vicinity of our trisaccharide for the stabilization of this sugar-lectin complex.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
12925992 Q.Vicens, and E.Westhof (2003).
Molecular recognition of aminoglycoside antibiotics by ribosomal RNA and resistance enzymes: an analysis of x-ray crystal structures.
  Biopolymers, 70, 42-57.  
  10210179 J.C.Rosa, P.S.De Oliveira, R.Garratt, L.Beltramini, K.Resing, M.C.Roque-Barreira, and L.J.Greene (1999).
KM+, a mannose-binding lectin from Artocarpus integrifolia: amino acid sequence, predicted tertiary structure, carbohydrate recognition, and analysis of the beta-prism fold.
  Protein Sci, 8, 13-24.  
10090286 M.M.Prabu, K.Suguna, and M.Vijayan (1999).
Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins.
  Proteins, 35, 58-69.  
10089310 N.Manoj, V.R.Srinivas, and K.Suguna (1999).
Structure of basic winged-bean lectin and a comparison with its saccharide-bound form.
  Acta Crystallogr D Biol Crystallogr, 55, 794-800.
PDB code: 1wbf
10417405 R.Ravishankar, K.Suguna, A.Surolia, and M.Vijayan (1999).
Structures of the complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins.
  Acta Crystallogr D Biol Crystallogr, 55, 1375-1382.
PDB codes: 1ciw 1qf3
9052976 J.M.Richardson, M.J.Milton, and S.W.Homans (1995).
Solution dynamics of the oligosaccharide moiety of ganglioside GM1: comparison of solution conformations with the bound state conformation in association with cholera toxin B-pentamer.
  J Mol Recognit, 8, 358-362.  
7696853 R.Loris, F.Casset, J.Bouckaert, J.Pletinckx, M.H.Dao-Thi, F.Poortmans, A.Imberty, S.Perez, and L.Wyns (1994).
The monosaccharide binding site of lentil lectin: an X-ray and molecular modelling study.
  Glycoconj J, 11, 507-517.
PDB code: 1lem
7873934 R.R.Van Eijsden, B.S.De Pater, and J.W.Kijne (1994).
Mutational analysis of the sugar-binding site of pea lectin.
  Glycoconj J, 11, 375-380.  
8069634 Y.Bourne, J.Mazurier, D.Legrand, P.Rougé, J.Montreuil, G.Spik, and C.Cambillau (1994).
Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety.
  Structure, 2, 209-219.
PDB codes: 1lgb 1lgc
8243456 H.Lis, and N.Sharon (1993).
Protein glycosylation. Structural and functional aspects.
  Eur J Biochem, 218, 1.  
1422132 A.Ayouba, H.Debray, and P.Rougé (1992).
Fine sugar specificity of the Butea frondosa seed lectin.
  Glycoconj J, 9, 141-147.  
1823622 A.Imberty, M.M.Delage, Y.Bourne, C.Cambillau, and S.Pérez (1991).
Data bank of three-dimensional structures of disaccharides: Part II, N-acetyllactosaminic type N-glycans. Comparison with the crystal structure of a biantennary octasaccharide.
  Glycoconj J, 8, 456-483.  
1841681 J.Mazurier, M.Dauchez, G.Vergoten, J.Montreuil, and G.Spik (1991).
Molecular modeling of a disialylated monofucosylated biantennary glycan of the N-acetyllactosamine type.
  Glycoconj J, 8, 390-399.  
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.

 

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