1HE9
Crystal structure of the GAP domain of the Pseudomonas aeruginosa ExoS toxin
Summary for 1HE9
| Entry DOI | 10.2210/pdb1he9/pdb |
| Related | 1HE1 |
| Descriptor | EXOENZYME S (2 entities in total) |
| Functional Keywords | toxin (exoenzyme s), exos, pseudomonas aeruginosa, gap, toxin, virulence factor, signal transduction |
| Biological source | PSEUDOMONAS AERUGINOSA |
| Total number of polymer chains | 1 |
| Total formula weight | 14432.83 |
| Authors | Wurtele, M.,Renault, L.,Barbieri, J.T.,Wittinghofer, A.,Wolf, E. (deposition date: 2000-11-21, release date: 2001-03-19, Last modification date: 2024-11-13) |
| Primary citation | Wurtele, M.,Renault, L.,Barbieri, J.T.,Wittinghofer, A.,Wolf, E. Structure of the Exos Gtpase Activating Domain FEBS Lett., 491:26-, 2001 Cited by PubMed Abstract: Pseudomonas aeruginosa is an opportunistic bacterial pathogen of great medical relevance. One of its major toxins, exoenzyme S (ExoS), is a dual function protein with a C-terminal Ras-ADP-ribosylation domain and an N-terminal GTPase activating protein (GAP) domain specific for Rho-family proteins. We report here the three-dimensional structure of the N-terminal domain of ExoS determined by X-ray crystallography to 2.4 A resolution. Its fold is all helical with a four helix bundle core capped by additional irregular helices. Loops that are known to interact with Rho-family proteins show very large mobility. Considering the importance of ExoS in Pseudomonas pathogenicity, this structure could be of interest for drug targeting. PubMed: 11226412DOI: 10.1016/S0014-5793(01)02105-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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