1he9
Crystal structure of the GAP domain of the Pseudomonas aeruginosa ExoS toxinCrystal structure of the GAP domain of the Pseudomonas aeruginosa ExoS toxin
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPseudomonas 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. Structure of the ExoS GTPase activating domain.,Wurtele M, Renault L, Barbieri JT, Wittinghofer A, Wolf E FEBS Lett. 2001 Feb 23;491(1-2):26-9. PMID:11226412[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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