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Toxin PDB id
1qxm
Jmol
Contents
Protein chains
283 a.a. *
Ligands
EDO ×7
Waters ×651
* Residue conservation analysis
PDB id:
1qxm
Name: Toxin
Title: Crystal structure of a hemagglutinin component (ha1) from typE C clostridium botulinum
Structure: Ha1. Chain: a, b. Fragment: hemagglutinin component ha1. Engineered: yes. Mutation: yes
Source: Clostridium botulinum d phage. Organism_taxid: 29342. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.70Å     R-factor:   0.177     R-free:   0.201
Authors: K.Inoue,M.Sobhany,T.R.Transue,K.Oguma,L.C.Pedersen,M.Negishi
Key ref: K.Inoue et al. (2003). Structural analysis by X-ray crystallography and calorimetry of a haemagglutinin component (HA1) of the progenitor toxin from Clostridium botulinum. Microbiology, 149, 3361-3370. PubMed id: 14663070 DOI: 10.1099/mic.0.26586-0
Date:
08-Sep-03     Release date:   20-Jan-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P46084  (HA33_CLOBO) -  Main hemagglutinin component
Seq:
Struc:
286 a.a.
283 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     sugar binding     1 term  

 

 
DOI no: 10.1099/mic.0.26586-0 Microbiology 149:3361-3370 (2003)
PubMed id: 14663070  
 
 
Structural analysis by X-ray crystallography and calorimetry of a haemagglutinin component (HA1) of the progenitor toxin from Clostridium botulinum.
K.Inoue, M.Sobhany, T.R.Transue, K.Oguma, L.C.Pedersen, M.Negishi.
 
  ABSTRACT  
 
Botulism food poisoning is caused primarily by ingestion of the Clostridium botulinum neurotoxin (BoNT). The 1300 amino acid BoNT forms a progenitor toxin (PTX) that, when associated with a number of other proteins, increases its oral toxicity by protecting it from the low pH of the stomach and from intestinal proteases. One of these associated proteins, HA1, has also been suggested to be involved with internalization of the toxin into the bloodstream by binding to oligosaccharides lining the intestine. Here is reported the crystal structure of HA1 from type C Clostridium botulinum at a resolution of 1.7 Angstrom. The protein consists of two beta-trefoil domains and bears structural similarities to the lectin B-chain from the deadly plant toxin ricin. Based on structural comparison to the ricin B-chain lactose-binding sites, residues of type A HA1 were selected and mutated. The D263A and N285A mutants lost the ability to bind carbohydrates containing galactose moieties, implicating these residues in carbohydrate binding.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20450284 N.J.Mantis, and S.J.Forbes (2010).
Secretory IgA: arresting microbial pathogens at epithelial borders.
  Immunol Invest, 39, 383-406.  
19292877 H.Hemmi, A.Kuno, S.Ito, R.Suzuki, T.Hasegawa, and J.Hirabayashi (2009).
NMR studies on the interaction of sugars with the C-terminal domain of an R-type lectin from the earthworm Lumbricus terrestris.
  FEBS J, 276, 2095-2105.  
19146895 R.J.Mrsny (2009).
Lessons from nature: "Pathogen-Mimetic" systems for mucosal nano-medicines.
  Adv Drug Deliv Rev, 61, 172-192.  
  18084087 T.Nakamura, T.Tonozuka, M.Kotani, K.Obata, K.Oguma, and A.Nishikawa (2007).
Crystallization and preliminary X-ray analysis of the HA3 component of Clostridium botulinum type C progenitor toxin.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 1038-1040.  
17076664 I.Carpusca, T.Jank, and K.Aktories (2006).
Bacillus sphaericus mosquitocidal toxin (MTX) and pierisin: the enigmatic offspring from the family of ADP-ribosyltransferases.
  Mol Microbiol, 62, 621-630.  
17009862 W.K.Kim, A.Henschel, C.Winter, and M.Schroeder (2006).
The many faces of protein-protein interactions: A compendium of interface geometry.
  PLoS Comput Biol, 2, e124.  
16140523 A.Imberty, E.P.Mitchell, and M.Wimmerová (2005).
Structural basis of high-affinity glycan recognition by bacterial and fungal lectins.
  Curr Opin Struct Biol, 15, 525-534.  
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.