4X3F

Crystal structure of the intracellular domain of the M. tuberculosis Ser/Thr kinase PknA

Summary for 4X3F

• Entry DOI: 10.2210/pdb4x3f/pdb
• Descriptor: Serine/threonine-protein kinase PknA, ... (4 entities in total)
• Functional Keywords: kinase, autoinhibition, phosphorylation, transferase
• Biological source: Mycobacterium tuberculosis; More
• Cellular location: Cell membrane ; Single-pass membrane protein : P9WI83 P9WI83 P9WI83
• Total number of polymer chains: 3
• Total formula weight: 107813.63

Authors

Wagner, T.,Wehenkel, A.,Alzari, P.M.,Bellinzoni, M. (deposition date: 2014-11-28, release date: 2015-01-21, Last modification date: 2024-01-10)

Primary citation

Wagner, T.,Alexandre, M.,Duran, R.,Barilone, N.,Wehenkel, A.,Alzari, P.M.,Bellinzoni, M.
The crystal structure of the catalytic domain of the ser/thr kinase PknA from M. tuberculosis shows an Src-like autoinhibited conformation.
Proteins, 83:982-988, 2015

PubMed Abstract: 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.

PubMed: 25586004
DOI: 10.1002/prot.24754

Experimental method

X-RAY DIFFRACTION (2.9 Å)