Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter

Detalhes bibliográficos
Autor(a) principal: Szollosi, A
Data de Publicação: 2016
Outros Autores: Vieira-Pires, RS, Teixeira-Duarte, C, Rocha, R, Morais-Cabral, JH
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10216/108245
Resumo: 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.
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spelling Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ TransporterC-di-ampMembrane region m-2c2Uptake system ktrabHuman bk channelVibrio-alginolyticusReceptor desensitizationStructural mechanismAngstrom resolutionGating ringRck domainKtrAB 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.Public Library of Science20162016-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10216/108245eng1544-917310.1371/journal.pbio.1002356Szollosi, AVieira-Pires, RSTeixeira-Duarte, CRocha, RMorais-Cabral, JHinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-29T13:58:46Zoai:repositorio-aberto.up.pt:10216/108245Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T23:51:26.059948Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter
title Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter
spellingShingle Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter
Szollosi, A
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
title_short Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter
title_full Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter
title_fullStr Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter
title_full_unstemmed Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter
title_sort Dissecting the Molecular Mechanism of Nucleotide-Dependent Activation of the KtrAB K+ Transporter
author Szollosi, A
author_facet Szollosi, A
Vieira-Pires, RS
Teixeira-Duarte, C
Rocha, R
Morais-Cabral, JH
author_role author
author2 Vieira-Pires, RS
Teixeira-Duarte, C
Rocha, R
Morais-Cabral, JH
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Szollosi, A
Vieira-Pires, RS
Teixeira-Duarte, C
Rocha, R
Morais-Cabral, JH
dc.subject.por.fl_str_mv 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
topic 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
description 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.
publishDate 2016
dc.date.none.fl_str_mv 2016
2016-01-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10216/108245
url http://hdl.handle.net/10216/108245
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1544-9173
10.1371/journal.pbio.1002356
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Public Library of Science
publisher.none.fl_str_mv Public Library of Science
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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