| Structural highlights
Function
[PKNA_MYCTU] Key component of a signal transduction pathway that regulates cell growth and cell division via phosphorylation of target proteins such as FtsZ, Wag31, GlmU, FhaB, PstP, EmbR and Rv1422. Shows a strong preference for Thr versus Ser as the phosphoacceptor.[1] [2] [3] [4] [5] [6]
Publication Abstract from PubMed
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. This article is protected by copyright. All rights reserved.
The crystal structure of the catalytic domain of the Ser/Thr kinase PknA from M. tuberculosis shows an Src-like autoinhibited conformation.,Wagner T, Alexandre M, Duran R, Barilone N, Wehenkel A, Alzari PM, Bellinzoni M Proteins. 2015 Jan 13. doi: 10.1002/prot.24754. PMID:25586004[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kang CM, Abbott DW, Park ST, Dascher CC, Cantley LC, Husson RN. The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape. Genes Dev. 2005 Jul 15;19(14):1692-704. Epub 2005 Jun 28. PMID:15985609 doi:https://dx.doi.org/10.1101/gad.1311105
- ↑ Sharma K, Gupta M, Krupa A, Srinivasan N, Singh Y. EmbR, a regulatory protein with ATPase activity, is a substrate of multiple serine/threonine kinases and phosphatase in Mycobacterium tuberculosis. FEBS J. 2006 Jun;273(12):2711-21. PMID:16817899 doi:https://dx.doi.org/10.1111/j.1742-4658.2006.05289.x
- ↑ Parikh A, Verma SK, Khan S, Prakash B, Nandicoori VK. PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity. J Mol Biol. 2009 Feb 20;386(2):451-64. Epub 2008 Dec 24. PMID:19121323 doi:10.1016/j.jmb.2008.12.031
- ↑ Sureka K, Hossain T, Mukherjee P, Chatterjee P, Datta P, Kundu M, Basu J. Novel role of phosphorylation-dependent interaction between FtsZ and FipA in mycobacterial cell division. PLoS One. 2010 Jan 6;5(1):e8590. doi: 10.1371/journal.pone.0008590. PMID:20066037 doi:https://dx.doi.org/10.1371/journal.pone.0008590
- ↑ Jani C, Eoh H, Lee JJ, Hamasha K, Sahana MB, Han JS, Nyayapathy S, Lee JY, Suh JW, Lee SH, Rehse SJ, Crick DC, Kang CM. Regulation of polar peptidoglycan biosynthesis by Wag31 phosphorylation in mycobacteria. BMC Microbiol. 2010 Dec 29;10:327. doi: 10.1186/1471-2180-10-327. PMID:21190553 doi:https://dx.doi.org/10.1186/1471-2180-10-327
- ↑ Sajid A, Arora G, Gupta M, Upadhyay S, Nandicoori VK, Singh Y. Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB. PLoS One. 2011 Mar 9;6(3):e17871. doi: 10.1371/journal.pone.0017871. PMID:21423706 doi:https://dx.doi.org/10.1371/journal.pone.0017871
- ↑ Wagner T, Alexandre M, Duran R, Barilone N, Wehenkel A, Alzari PM, 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. 2015 Jan 13. doi: 10.1002/prot.24754. PMID:25586004 doi:https://dx.doi.org/10.1002/prot.24754
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