ABC transporters: a riddle wrapped in a mystery inside an enigma

Jones, PM; O'Mara, ML; George, AM

ABC transporters: a riddle wrapped in a mystery inside an enigma

Jones, PM O'Mara, ML George, AM

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Publication Type:: Journal Article
Citation:: Trends in Biochemical Sciences, 2009, 34 (10), pp. 520 - 531
Issue Date:: 2009-10-01

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Field	Value	Language
dc.contributor.author	Jones, PM	en_US
dc.contributor.author	O'Mara, ML	en_US
dc.contributor.author	George, AM https://orcid.org/0000-0003-4691-8960	en_US
dc.date.available	2009-06-24	en_US
dc.date.issued	2009-10-01	en_US
dc.identifier.citation	Trends in Biochemical Sciences, 2009, 34 (10), pp. 520 - 531	en_US
dc.identifier.issn	0968-0004	en_US
dc.identifier.uri	http://hdl.handle.net/10453/8676
dc.description.abstract	ATP-binding cassette (ABC) transporters form one of the largest and most ancient of protein families. ABC transporters couple hydrolysis of ATP to vectorial translocation of diverse substrates across cellular membranes. Many human ABC transporters are medically important in causing, for example, multidrug resistance to cytotoxic drugs. Seven complete prokaryotic structures and one eukaryotic structure have been solved for transporters from 2002 to date, and a wealth of research is being conducted on and around these structures to resolve the mechanistic conundrum of how these transporters couple ATP hydrolysis in cytosolic domains to substrate translocation through the transmembrane pore. Many questions remained unanswered about this mechanism, despite a plethora of data and a number of interesting and controversial models. © 2009 Elsevier Ltd. All rights reserved.	en_US
dc.relation.ispartof	Trends in Biochemical Sciences	en_US
dc.relation.isbasedon	10.1016/j.tibs.2009.06.004	en_US
dc.subject.classification	Developmental Biology	en_US
dc.subject.mesh	Humans	en_US
dc.subject.mesh	Molybdenum	en_US
dc.subject.mesh	Metals	en_US
dc.subject.mesh	Maltose	en_US
dc.subject.mesh	Methionine	en_US
dc.subject.mesh	ATP-Binding Cassette Transporters	en_US
dc.subject.mesh	Adenosine Triphosphate	en_US
dc.subject.mesh	Crystallography, X-Ray	en_US
dc.subject.mesh	Evolution, Molecular	en_US
dc.subject.mesh	Binding Sites	en_US
dc.subject.mesh	Protein Conformation	en_US
dc.subject.mesh	Biological Transport	en_US
dc.subject.mesh	Models, Molecular	en_US
dc.title	ABC transporters: a riddle wrapped in a mystery inside an enigma	en_US
dc.type	Journal Article
utslib.citation.volume	10	en_US
utslib.citation.volume	34	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	0903 Biomedical Engineering	en_US
utslib.for	03 Chemical Sciences	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
utslib.copyright.status	open_access
pubs.issue	10	en_US
pubs.publication-status	Published	en_US
pubs.volume	34	en_US

Abstract:

ATP-binding cassette (ABC) transporters form one of the largest and most ancient of protein families. ABC transporters couple hydrolysis of ATP to vectorial translocation of diverse substrates across cellular membranes. Many human ABC transporters are medically important in causing, for example, multidrug resistance to cytotoxic drugs. Seven complete prokaryotic structures and one eukaryotic structure have been solved for transporters from 2002 to date, and a wealth of research is being conducted on and around these structures to resolve the mechanistic conundrum of how these transporters couple ATP hydrolysis in cytosolic domains to substrate translocation through the transmembrane pore. Many questions remained unanswered about this mechanism, despite a plethora of data and a number of interesting and controversial models. © 2009 Elsevier Ltd. All rights reserved.

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http://hdl.handle.net/10453/8676