Structural diversity of ABC transporters

ATP-binding cassette (ABC) transporters form a large superfamily of ATP-dependent protein complexes that mediate transport of a vast array of substrates across membranes. The 14 currently available structures of ABC transporters have greatly advanced insight into the transport mechanism and revealed...

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Detalles Bibliográficos
Autores principales: ter Beek, Josy, Guskov, Albert, Slotboom, Dirk Jan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2014
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3971661/
https://www.ncbi.nlm.nih.gov/pubmed/24638992
http://dx.doi.org/10.1085/jgp.201411164
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author ter Beek, Josy
Guskov, Albert
Slotboom, Dirk Jan
author_facet ter Beek, Josy
Guskov, Albert
Slotboom, Dirk Jan
author_sort ter Beek, Josy
collection PubMed
description ATP-binding cassette (ABC) transporters form a large superfamily of ATP-dependent protein complexes that mediate transport of a vast array of substrates across membranes. The 14 currently available structures of ABC transporters have greatly advanced insight into the transport mechanism and revealed a tremendous structural diversity. Whereas the domains that hydrolyze ATP are structurally related in all ABC transporters, the membrane-embedded domains, where the substrates are translocated, adopt four different unrelated folds. Here, we review the structural characteristics of ABC transporters and discuss the implications of this structural diversity for mechanistic diversity.
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spelling pubmed-39716612014-10-01 Structural diversity of ABC transporters ter Beek, Josy Guskov, Albert Slotboom, Dirk Jan J Gen Physiol Review ATP-binding cassette (ABC) transporters form a large superfamily of ATP-dependent protein complexes that mediate transport of a vast array of substrates across membranes. The 14 currently available structures of ABC transporters have greatly advanced insight into the transport mechanism and revealed a tremendous structural diversity. Whereas the domains that hydrolyze ATP are structurally related in all ABC transporters, the membrane-embedded domains, where the substrates are translocated, adopt four different unrelated folds. Here, we review the structural characteristics of ABC transporters and discuss the implications of this structural diversity for mechanistic diversity. The Rockefeller University Press 2014-04 /pmc/articles/PMC3971661/ /pubmed/24638992 http://dx.doi.org/10.1085/jgp.201411164 Text en © 2014 ter Beek et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Review
ter Beek, Josy
Guskov, Albert
Slotboom, Dirk Jan
Structural diversity of ABC transporters
title Structural diversity of ABC transporters
title_full Structural diversity of ABC transporters
title_fullStr Structural diversity of ABC transporters
title_full_unstemmed Structural diversity of ABC transporters
title_short Structural diversity of ABC transporters
title_sort structural diversity of abc transporters
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3971661/
https://www.ncbi.nlm.nih.gov/pubmed/24638992
http://dx.doi.org/10.1085/jgp.201411164
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