Alternative proton-binding site and long-distance coupling in Escherichia coli sodium-proton antiporter NhaA.

doi:10.1073/pnas.2005467117

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Article

Alternative proton-binding site and long-distance coupling in Escherichia coli sodium-proton antiporter NhaA.

Proceedings of the National Academy of Sciences of the United States of America - 13 Oct 2020

Henderson Jack A, Huang Yandong, Beckstein Oliver, Shen Jana

Abstract excerpt

Escherichia coli NhaA is a prototypical sodium-proton antiporter responsible for maintaining cellular ion and volume homeostasis by exchanging two protons for one sodium ion; despite two decades of research, the transport mechanism of NhaA remains poorly understood. Recent crystal structure and computational studies suggested Lys300 as a second proton-binding site; however, functional measurements of several K300...

Topics

Aspartic Acid
Binding Sites
Escherichia coli Proteins
Hydrogen Bonding
Lysine
Molecular Dynamics Simulation
Mutation
Protons
Sodium-Hydrogen Exchangers
Static Electricity

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Identifiers

PMID: 32973095
DOI: 10.1073/pnas.2005467117
PMCID: PMC7568328

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