Related Experiment Video
Updated: Sep 27, 2026

A Guide to Production, Crystallization, and Structure Determination of Human IKK1/α
Published on: November 2, 2018
Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases
Tracy A Young1, Benedicte Delagoutte, James A Endrizzi
1Department of Molecular and Cell Biology, 229 Stanley Hall 3206, University of California, Berkeley, California 94720-3206, USA.
Abstract:
A family of eukaryotic-like Ser/Thr protein kinases occurs in bacteria, but little is known about the structures and functions of these proteins. Here we characterize PknB, a transmembrane signaling kinase from Mycobacterium tuberculosis. The intracellular PknB kinase domain is active autonomously, and the active enzyme is phosphorylated on residues homologous to regulatory phospho-acceptors in eukaryotic Ser/Thr kinases. The crystal structure of the PknB kinase domain in complex with an ATP analog reveals the active conformation. The predicted fold of the PknB extracellular domain matches the proposed targeting domain of penicillin-binding protein 2x. The structural and chemical similarities of PknB to metazoan homologs support a universal activation mechanism of Ser/Thr protein kinases in prokaryotes and eukaryotes.
Related Concept Videos
MAPK Signaling Cascades
PI3K/mTOR/AKT Signaling Pathway
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The JAK-STAT Signaling Pathway
Amplifying Signals via Enzymatic Cascade
cAMP-dependent Protein Kinase Pathways

