Please use this identifier to cite or link to this item: http://hdl.handle.net/10216/108245
Author(s): Szollosi, A
Vieira-Pires, RS
Teixeira-Duarte, C
Rocha, R
Morais-Cabral, JH
Title: Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter
Publisher: Public Library of Science
Issue Date: 2016
Abstract: KtrAB belongs to the Trk/Ktr/HKT superfamily of monovalent cation (K+ and Na+) transport proteins that closely resemble K+ channels. These proteins underlie a plethora of cellular functions that are crucial for environmental adaptation in plants, fungi, archaea, and bacteria. The activation mechanism of the Trk/Ktr/HKT proteins remains unknown. It has been shown that ATP stimulates the activity of KtrAB while ADP does not. Here, we present X-ray structural information on the KtrAB complex with bound ADP. A comparison with the KtrAB-ATP structure reveals conformational changes in the ring and in the membrane protein. In combination with a biochemical and functional analysis, we uncover how ligand- dependent changes in the KtrA ring are propagated to the KtrB membrane protein and conclude that, despite their structural similarity, the activation mechanism of KtrAB is markedly different from the activation mechanism of K+ channels.
Subject: C-di-amp
Membrane region m-2c2
Uptake system ktrab
Human bk channel
Vibrio-alginolyticus
Receptor desensitization
Structural mechanism
Angstrom resolution
Gating ring
Rck domain
URI: http://hdl.handle.net/10216/108245
Source: PLoS Biology, vol. 14 (1):e1002356
Related Information: info:eu-repo/grantAgreement/FCT/COMPETE/127520/PT
Document Type: Artigo em Revista Científica Internacional
Rights: openAccess
License: http://creativecommons.org/licenses/by/4.0/
Appears in Collections:I3S - Artigo em Revista Científica Internacional

Files in This Item:
File Description SizeFormat 
journal.pbio.1002356.pdf2.44 MBAdobe PDFThumbnail
View/Open


This item is licensed under a Creative Commons License Creative Commons