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Physiological, Structural, and Functional Analysis of the Paralogous Cation-Proton Antiporters of NhaP Type from Vibrio cholerae
Ist Teil von
International journal of molecular sciences, 2019-05, Vol.20 (10), p.2572
Ort / Verlag
Switzerland: MDPI AG
Erscheinungsjahr
2019
Quelle
EZB Electronic Journals Library
Beschreibungen/Notizen
The transmembrane K
/H
antiporters of NhaP type of
(Vc-NhaP1, 2, and 3) are critical for maintenance of K
homeostasis in the cytoplasm. The entire functional NhaP group is indispensable for the survival of
at low pHs suggesting their possible role in the acid tolerance response (ATR) of
. Our findings suggest that the Vc-NhaP123 group, and especially its major component, Vc-NhaP2, might be a promising target for the development of novel antimicrobials by narrowly targeting
and other NhaP-expressing pathogens. On the basis of Vc-NhaP2 in silico structure modeling, Molecular Dynamics Simulations, and extensive mutagenesis studies, we suggest that the ion-motive module of Vc-NhaP2 is comprised of two functional regions: (i) a putative cation-binding pocket that is formed by antiparallel unfolded regions of two transmembrane segments (TMSs V/XII) crossing each other in the middle of the membrane, known as the NhaA fold; and (ii) a cluster of amino acids determining the ion selectivity.