title: Kinase Regulation in Mycobacterium tuberculosis: Variations on a Theme.
abstract: In this issue of Structure, Lisa et al. (2015) examine how the PknG protein kinase of M. tuberculosis efficiently binds and phosphorylates substrates. The work highlights interesting parallels between PknG and eukaryotic protein kinases.
authors.affiliation: Swiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne 1015, Switzerland.
authors.forename: Sina
authors.initials: S
authors.lastname: Reckel
authors.affiliation: Swiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne 1015, Switzerland. Electronic address: oliver.hantschel@epfl.ch.
authors.forename: Oliver
authors.initials: O
authors.lastname: Hantschel
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D015971:Gene Expression Regulation, Enzymologic / Q000235:genetics*; D008958:Models, Molecular; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D017346:Protein Serine-Threonine Kinases