Essential ion binding residues for Na+ flow in stator complex of the Vibrio flagellar motor

Scientific Reports
Yasuhiro OnoueMichio Homma

Abstract

The bacterial flagellar motor is a unique supramolecular complex which converts ion flow into rotational force. Many biological devices mainly use two types of ions, proton and sodium ion. This is probably because of the fact that life originated in seawater, which is rich in protons and sodium ions. The polar flagellar motor in Vibrio is coupled with sodium ion and the energy converting unit of the motor is composed of two membrane proteins, PomA and PomB. It has been shown that the ion binding residue essential for ion transduction is the conserved aspartic acid residue (PomB-D24) in the PomB transmembrane region. To reveal the mechanism of ion selectivity, we identified essential residues, PomA-T158 and PomA-T186, other than PomB-D24, in the Na+-driven flagellar motor. It has been shown that the side chain of threonine contacts Na+ in Na+-coupled transporters. We monitored the Na+-binding specific structural changes using ATR-FTIR spectroscopy. The signals were abolished in PomA-T158A and -T186A, as well as in PomB-D24N. Molecular dynamics simulations further confirmed the strong binding of Na+ to D24 and showed that T158A and T186A hindered the Na+ binding and transportation. The data indicate that two threonine residues (P...Continue Reading

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Citations

Jul 1, 2020·Annual Review of Microbiology·Judith P Armitage, Richard M Berry
Jan 12, 2021·Frontiers in Microbiology·Md Imtiazul IslamMatthew A B Baker
Sep 16, 2020·Cell·Mònica SantiveriNicholas M I Taylor
Jul 24, 2021·Trends in Biochemical Sciences·Haidai HuNicholas M I Taylor

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Methods Mentioned

BETA
light microscopy
motility assay
X-ray

Software Mentioned

- tr / 2D
Modeller
NAMD
Procheck
SMD
embed
CLUSTAL Omega
Move

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