Structure of the ExoS GTPase activating domain

FEBS Letters

Renault, Louis¹  Würtele, Martin¹  Wolf, Eva¹  Barbieri, Joseph T.²  Wittinghofer, Alfred¹ 

[1] Max-Planck-Institut für molekulare Physiologie, Abteilung Strukturelle Biologie, Otto-Hahn-Str. 11, 44227 Dortmund, Germany;Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, WI 53226, USA

关键词: Toxin;    ExoS;    GTPase activating protein;    X-ray structure;    Pseudomonas aeruginosa;    ExoS;    exoenzyme S;    GAP;    GTPase activating protein;    MAD;    multiwavelength anomalous dispersion;    GEF;    guanine-nucleotide exchange factor;    r.m.s.;    root mean square;   

DOI  :  10.1016/S0014-5793(01)02105-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown