 |
|
| PROSITE documentation PDOC51074 [for PROSITE entry PS51074] |
Zinc finger DPH-type profile
Diphthamide is a unique post-translationally modified histidine residue found only in translation elongation factor 2 (eEF-2). It is conserved from archaebacteria to humans and serves as the target for diphteria toxin and Pseudomonas exotoxin A. These two toxins catalyze the transfer of ADP-ribose to diphtamide on eEF-2, thus inactivating eEF-2, halting cellular protein synthesis, and causing cell death [1].
The biosynthesis of diphtamide is dependent on at least five proteins, DPH1 to -5, and a still unidentified amidating enzyme. DPH3 and DPH4 share a conserved region which encode a putative zinc finger, the DHP-type or CSL-type (after the conserved motif of the final cysteine) zinc finger [2,3]. The function of this motif is unknown.
The profile we developed covers the whole DPH-type zinc finger.
Last update:January 2005 / First entry.
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Collier R.J. |
| Title | Understanding the mode of action of diphtheria toxin: a perspective on progress during the 20th century. | |
| Source | Toxicon 39:1793-1803(2001). | |
| PubMed ID | 11595641 |
| 2 | Authors | Liu S. Leppla S.H. |
| Title | Retroviral insertional mutagenesis identifies a small protein required for synthesis of diphthamide, the target of bacterial ADP-ribosylating toxins. | |
| Source | Mol. Cell 12:603-613(2003). | |
| PubMed ID | 14527407 |
| 3 | Authors | Liu S. Milne G.T. Kuremsky J.G. Fink G.R. Leppla S.H. |
| Title | Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. | |
| Source | Mol. Cell. Biol. 24:9487-9497(2004). | |
| PubMed ID | 15485916 | |
| DOI | 10.1128/MCB.24.21.9487-9497.2004 |
PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to Prosite License or see: prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)