Structural insights into the functional versatility of an FHA domain protein in mycobacterial signaling-Reference-Cited by-同舟云学术

Structural insights into the functional versatility of an FHA domain protein in mycobacterial signaling

Published:2019-05-07 Issue:580 Volume:12 Page:
ISSN:1945-0877
Container-title:Science Signaling
language:en
Short-container-title:Sci. Signal.

Author:

Wagner Tristan¹^ORCID,André-Leroux Gwénaëlle¹^ORCID,Hindie Valérie¹,Barilone Nathalie¹,Lisa María-Natalia¹^ORCID,Hoos Sylviane²,Raynal Bertrand²,Vulliez-Le Normand Brigitte¹,O’Hare Helen M.³,Bellinzoni Marco¹^ORCID,Alzari Pedro M.¹^ORCID

Affiliation:

1. Institut Pasteur, Unité de Microbiologie Structurale, CNRS UMR 3528 & Université Paris Diderot, 25 Rue du Docteur Roux, 75724 Paris Cedex 15, France.

2. Institut Pasteur, Plateforme de Biophysique Moléculaire, 25 Rue du Docteur Roux, 75724 Paris Cedex 15, France.

3. Leicester Tuberculosis Research Group (LTBRG) and Leicester Institute of Structural and Chemical Biology (LISCB), Department of Respiratory Science & Department of Molecular and Cell Biology, University of Leicester, Leicester LE1 7RH, UK.

Abstract

The FHA domain of mycobacterial GarA mediates interactions with both phosphorylated and nonphosphorylated partners.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference65 articles.

1. Mycobacterial Ser/Thr protein kinases and phosphatases: Physiological roles and therapeutic potential

2. Eukaryote-Like Serine/Threonine Kinases and Phosphatases in Bacteria

3. Protein phosphorylation in bacterial signal transduction

4. Reading protein modifications with interaction domains

5. Modular evolution of phosphorylation-based signalling systems

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