CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.175 | Diphtheria Toxin; domain 1 |
|
3.90.175.10 | Diphtheria Toxin, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Diphtheria Toxin, domain 1 |
| Functional Family |
Enzyme Information
| 2.4.2.36 |
NAD(+)--diphthamide ADP-ribosyltransferase.
based on mapping to UniProt Q5EK40
NAD(+) + diphthamide-[translation elongation factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2].
-!- Dihtheria toxin and some other bacterial toxins catalyze this reaction, which inactivates translation elongation factor 2 (EF2). -!- The acceptor is diphthamide, a unique modification of a histidine residue in the elongation factor found in archaebacteria and all eukaryotes, but not in eubacteria. -!- Cf. EC 2.4.2.31. -!- The relevant histidine of EF2 is His(715) in mammals, His(699) in yeast and His(600) in Pyrococcus horikoshii.
|
UniProtKB Entries (1)
| Q5EK40 |
CHXA_VIBCL
Vibrio cholerae
Cholix toxin
|
PDB Structure
| PDB | 3NY6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Newly discovered and characterized antivirulence compounds inhibit bacterial mono-ADP-ribosyltransferase toxins.
Antimicrob.Agents Chemother.
|