LipidII interaction with specific residues of Mycobacterium tuberculosis PknB extracytoplasmic domain governs its optimal activation
The Mycobacterium tuberculosis kinase PknB regulates essential cell functions via interactions with muropeptides. Here the authors identify interaction sites in the extracytoplasmic PASTA domain and show that abrogation of ligand binding leads to a hyper-activated kinase, causing loss of homeostasis...
Main Authors: | Prabhjot Kaur, Marvin Rausch, Basanti Malakar, Uchenna Watson, Nikhil P. Damle, Yogesh Chawla, Sandhya Srinivasan, Kanika Sharma, Tanja Schneider, Gagan Deep Jhingan, Deepak Saini, Debasisa Mohanty, Fabian Grein, Vinay Kumar Nandicoori |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2019-03-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-019-09223-9 |
Similar Items
-
The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization.
by: Mushtaq Mir, et al.
Published: (2011-07-01) -
Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA and PknB.
by: Andaleeb Sajid, et al.
Published: (2011-03-01) -
Antimycobacterial and PknB Inhibitory Activities of Venezuelan Medicinal Plants
by: C. A. Aranaga, et al.
Published: (2020-01-01) -
Structural analysis of Staphylococcus aureus serine/threonine kinase PknB.
by: Sonja Rakette, et al.
Published: (2012-01-01) -
Staphylococcal PknB as the first prokaryotic representative of the proline-directed kinases.
by: Malgorzata Miller, et al.
Published: (2010-02-01)