The KdpC subunit of the Escherichia coli K+-transporting KdpB P-type ATPase acts as a catalytic chaperone
Author:
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2011.08224.x/fullpdf
Reference28 articles.
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2. The extremely halophilic archaeon Halobacterium salinarum R1 responds to potassium limitation by expression of the K+-transporting KdpFABC P-type ATPase and by a decrease in intracellular K+;Strahl;Extremophiles,2008
3. Towards an understanding of the molecular mechanisms of stimulus perception and signal transduction by the KdpD/KdpE system of Escherichia coli;Jung;J Mol Microbiol Biotechnol,2002
4. K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a functional and structural dimer;Heitkamp;Biochemistry,2008
5. Solution structure of the KdpFABC P-type ATPase from Escherichia coli by electron microscopic single particle analysis;Heitkamp;J Struct Biol,2009
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2. The KdpFABC complex – K+transport against all odds;Molecular Membrane Biology;2019-01-01
3. The Genomic Potentials of NOB and Comammox Nitrospira in River Sediment Are Impacted by Native Freshwater Mussels;Frontiers in Microbiology;2018-09-04
4. Crystal structure of the potassium-importing KdpFABC membrane complex;Nature;2017-06
5. Endogenous and Exogenous KdpF Peptide Increases Susceptibility of Mycobacterium bovis BCG to Nitrosative Stress and Reduces Intramacrophage Replication;Frontiers in Cellular and Infection Microbiology;2017-04-06
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