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...

Full description

Bibliographic Details
Main Authors:	ter Beek, Josy, Guskov, Albert, Slotboom, Dirk Jan
Format:	Online
Language:	English
Published:	The Rockefeller University Press 2014
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3971661/

id	pubmed-3971661
recordtype	oai_dc
spelling	pubmed-39716612014-10-01 Structural diversity of ABC transporters ter Beek, Josy Guskov, Albert Slotboom, Dirk Jan 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/).
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	ter Beek, Josy Guskov, Albert Slotboom, Dirk Jan
spellingShingle	ter Beek, Josy Guskov, Albert Slotboom, Dirk Jan Structural diversity of ABC transporters
author_facet	ter Beek, Josy Guskov, Albert Slotboom, Dirk Jan
author_sort	ter Beek, Josy
title	Structural diversity of ABC transporters
title_short	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_sort	structural diversity of abc transporters
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.
publisher	The Rockefeller University Press
publishDate	2014
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3971661/
_version_	1612072919086661632

Structural diversity of ABC transporters

Similar Items