Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 83, Issue 5, Pages 982-988Publisher
WILEY-BLACKWELL
DOI: 10.1002/prot.24754
Keywords
Mycobacterium tuberculosis; Ser; Thr phosphorylation; autophosphorylation; autoinhibition; X-ray crystallography; mass spectrometry
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Funding
- European Commission [LSHP-CT-2005-018923]
- Institut Pasteur
- CNRS
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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. Proteins 2015; 83:982-988. (c) 2015 Wiley Periodicals, Inc.
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