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Structure of the ExoS GTPase activating domain
Author(s) -
Würtele Martin,
Renault Louis,
Barbieri Joseph T.,
Wittinghofer Alfred,
Wolf Eva
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02105-6
Subject(s) - gtpase , helix bundle , pseudomonas aeruginosa , chemistry , domain (mathematical analysis) , protein structure , crystallography , protein family , microbiology and biotechnology , biophysics , stereochemistry , biology , biochemistry , bacteria , genetics , mathematical analysis , mathematics , gene
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 Å 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.