5ELE
Cholera toxin El Tor B-pentamer in complex with A Lewis-y
Summary for 5ELE
Entry DOI | 10.2210/pdb5ele/pdb |
Related PRD ID | PRD_900128 |
Descriptor | Cholera enterotoxin subunit B, alpha-L-fucopyranose-(1-2)-[2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-alpha-D-glucopyranose, CALCIUM ION, ... (8 entities in total) |
Functional Keywords | cholera toxin b-pentamer, a lewis-y, complex, blood group oligosaccharide/antigen, toxin |
Biological source | Vibrio cholerae O1 |
Cellular location | Secreted: P01556 |
Total number of polymer chains | 10 |
Total formula weight | 122388.56 |
Authors | Heggelund, J.E.,Burschowsky, D.,Krengel, U. (deposition date: 2015-11-04, release date: 2016-03-30, Last modification date: 2024-11-13) |
Primary citation | Heggelund, J.E.,Burschowsky, D.,Bjrnestad, V.A.,Hodnik, V.,Anderluh, G.,Krengel, U. High-Resolution Crystal Structures Elucidate the Molecular Basis of Cholera Blood Group Dependence. Plos Pathog., 12:e1005567-e1005567, 2016 Cited by PubMed 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. PubMed: 27082955DOI: 10.1371/journal.ppat.1005567 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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