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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Proteins

The crystal structure of the catalytic domain of the ser/thr kinase PknA from M. tuberculosis shows an Src-like autoinhibited conformation.

Team: Structural Microbiology
Team: Structural biology of metabolic enzymes and complexes
Team: Channel Receptors
Member: Pedro Alzari
Member: Marco Bellinzoni
Member: Anne Marie Wehenkel
Member: Nathalie Barilone
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Proteins - 25 Mar 2015

Wagner T, Alexandre M, Duran R, Barilone N, Wehenkel A, Alzari PM, Bellinzoni M,

Link to Pubmed [PMID] – 25586004

Link to DOI – 10.1002/prot.24754

Proteins 2015 May; 83(5): 982-8

Signal transduction mediated by Ser/Thr phosphorylation in Mycobacterium tuberculosis has been intensively studied in the last years, as its genome harbors eleven genes coding for eukaryotic-like Ser/Thr kinases. Here we describe the crystal structure and the autophosphorylation sites of the catalytic domain of PknA, one of two protein kinases essential for pathogen’s survival. The structure of the ligand-free kinase domain shows an auto-inhibited conformation similar to that observed in human Tyr kinases of the Src-family. These results reinforce the high conservation of structural hallmarks and regulation mechanisms between prokaryotic and eukaryotic protein kinases.