Diphtheria toxin

spinqualitylabelsall models Structure of diphtheria toxin complex with adenylyl-UMP (PDB code 1ddt). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Diphtheria toxin (DT) is a toxin which is secreted by the bacteria causing diphtheria. DT catalyzes the transfer of NAD to a diphthamide residue in the elongation factor-2 and thus inhibiting protein synthesis. See also Toxins. Disease A lethal dose of DT is ca. 0.1 μg per 1 kg of bodyweight. Relevance DT is used in several drugs as chemotherapeutic agent and as an immunotoxin. Structural highlights The biological assembly of Diphtheria toxin is dimer. DT is proteolitically cleaved into 2 fragments. Fragment A contains the catalytic domain (C) and fragment B contains the transmembrane (T) and receptor-binding (R) domains. DT active site is located in a cleft in the C domain. Water molecules are shown as red spheres. The 2 monomers of DT interact by domain swapping to form a compact, globular dimer structure.

3D structures of diphtheria toxin

Updated on 14-April-2025

{"openlevels":0}

• Diphtheria toxin
  • Toxins, 4ow6, 7k7b, 7k7c, 7k7d, 7k7e – CbDT – Corynebacterium diphtheriae
    
  • 4ae0, 5i82, 8g0f, 8g0g – CdDT (mutant)
    
• Diphtheria toxin complex
  • 1ddt, 1mdt, 1f0l – CdDT + adenylyl phosphor-UMP
    
  • 1tox – CdDT + NAD
    
  • 4ae1 – CdDT (mutant) + nicotinamide
    
  • 1xdt – CdDT + heparin-binding epidermal growth factor
    
  • 1dtp – CdDT catalytic domain + adenylyl phosphor-UMP
    

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman