Arginine Residue at Position 573 in Enterococcus hirae Vacuolar-type ATPase NtpI Subunit Plays a Crucial Role in Na+ Translocation
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference43 articles.
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1. Off-axis rotor in Enterococcus hirae V-ATPase visualized by Zernike phase plate single-particle cryo-electron microscopy;Scientific Reports;2018-10-23
2. Mutagenesis of the Residues Forming an Ion Binding Pocket of the NtpK Subunit of Enterococcus hirae V-ATPase;Journal of Bacteriology;2012-06-22
3. Structure of the rotor ring modified with N,N'-dicyclohexylcarbodiimide of the Na+-transporting vacuolar ATPase;Proceedings of the National Academy of Sciences;2011-08-03
4. Significance of the Glutamate-139 Residue of the V-Type Na+-ATPase NtpK Subunit in Catalytic Turnover Linked with Salt Tolerance of Enterococcus hirae;Journal of Bacteriology;2011-05-20
5. Evolutionary origins of membrane proteins;Structural Bioinformatics of Membrane Proteins;2010
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