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PDBsum entry 5elc

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protein ligands metals Protein-protein interface(s) links
Toxin PDB id
5elc

 

 

 

 

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Contents
Protein chains
(+ 4 more) 103 a.a.
Ligands
NDG-GAL-FUC-FUC ×4
NDG ×3
NAG ×3
GAL-FUC ×3
FUC ×4
NAG-GAL-FUC-FUC ×2
BCN ×10
Metals
_CA ×10
Waters ×656
PDB id:
5elc
Name: Toxin
Title: Cholera toxin el tor b-pentamer in complex with lewis-y
Structure: Cholera enterotoxin subunit b. Chain: a, b, c, d, e, f, g, h, i, j. Synonym: cholera enterotoxin b chain,cholera enterotoxin gamma chain, choleragenoid. Engineered: yes
Source: Vibrio cholerae o1. Organism_taxid: 127906. Gene: ctxb, toxb, vc_1456. Expressed in: vibrio. Expression_system_taxid: 662.
Resolution:
1.50Å     R-factor:   0.223     R-free:   0.260
Authors: J.E.Heggelund,D.Burschowsky,U.Krengel
Key ref: J.E.Heggelund et al. (2016). High-Resolution Crystal Structures Elucidate the Molecular Basis of Cholera Blood Group Dependence. Plos Pathog, 12, e1005567. PubMed id: 27082955 DOI: 10.1371/journal.ppat.1005567
Date:
04-Nov-15     Release date:   30-Mar-16    
PROCHECK
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 Headers
 References

Protein chains
P01556  (CHTB_VIBCH) -  Cholera enterotoxin subunit B from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Seq:
Struc:
124 a.a.
103 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1371/journal.ppat.1005567 Plos Pathog 12:e1005567 (2016)
PubMed id: 27082955  
 
 
High-Resolution Crystal Structures Elucidate the Molecular Basis of Cholera Blood Group Dependence.
J.E.Heggelund, D.Burschowsky, V.A.Bjørnestad, V.Hodnik, G.Anderluh, U.Krengel.
 
  ABSTRACT  
 
Cholera is the prime example of blood-group-dependent diseases, with individuals of blood group O experiencing the most severe symptoms. The cholera toxin is the main suspect to cause this relationship. We report the high-resolution crystal structures (1.1-1.6 Å) of the native cholera toxin B-pentamer for both classical and El Tor biotypes, in complexes with relevant blood group determinants and a fragment of its primary receptor, the GM1 ganglioside. The blood group A determinant binds in the opposite orientation compared to previously published structures of the cholera toxin, whereas the blood group H determinant, characteristic of blood group O, binds in both orientations. H-determinants bind with higher affinity than A-determinants, as shown by surface plasmon resonance. Together, these findings suggest why blood group O is a risk factor for severe cholera.
 

 

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