Is the Emperor Wearing Shorts? The Published Structures of ABC transporters.

Jones, P; George, AM

Is the Emperor Wearing Shorts? The Published Structures of ABC transporters.

Jones, P George, AM

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Publisher:: WILEY
Publication Type:: Journal Article
Citation:: FEBS letters, 2020
Issue Date:: 2020-09-27

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Field	Value	Language
dc.contributor.author	Jones, P
dc.contributor.author	George, AM
dc.date.accessioned	2020-12-17T01:07:32Z
dc.date.available	2020-09-13
dc.date.available	2020-12-17T01:07:32Z
dc.date.issued	2020-09-27
dc.identifier.citation	FEBS letters, 2020
dc.identifier.issn	0014-5793
dc.identifier.issn	1873-3468
dc.identifier.uri	http://hdl.handle.net/10453/144788
dc.description.abstract	ABC transporters use the energy of ATP binding and hydrolysis to transport substrates across cellular membranes. They comprise two highly conserved nucleotide binding domains and two transmembrane domains that form the transmembrane channel and contain the substrate binding sites. Structural analyses have found a variety of seemingly unrelated folds for the ABC transporter transmembrane domains, and from these a set of diverse mechanistic models has been inferred. Nevertheless, in spite of the explosion in structure determination of ABC transporters in the last decade, advancement in certainty and clarity as to fundamental aspects of their molecular mechanisms remains elusive. With this in mind, here we put and examine the question: Could current ABC structures differ from the physiologic membrane-embedded forms?
dc.format	Print-Electronic
dc.language	eng
dc.publisher	WILEY
dc.relation.ispartof	FEBS letters
dc.relation.isbasedon	10.1002/1873-3468.13941
dc.rights	info:eu-repo/semantics/restrictedAccess
dc.subject	0304 Medicinal and Biomolecular Chemistry, 0601 Biochemistry and Cell Biology, 0603 Evolutionary Biology
dc.subject.classification	Biochemistry & Molecular Biology
dc.title	Is the Emperor Wearing Shorts? The Published Structures of ABC transporters.
dc.type	Journal Article
utslib.location.activity	England
utslib.for	0304 Medicinal and Biomolecular Chemistry
utslib.for	0601 Biochemistry and Cell Biology
utslib.for	0603 Evolutionary Biology
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney
utslib.copyright.status	closed_access	*
dc.date.updated	2020-12-17T01:07:28Z
pubs.publication-status	Published

Abstract:

ABC transporters use the energy of ATP binding and hydrolysis to transport substrates across cellular membranes. They comprise two highly conserved nucleotide binding domains and two transmembrane domains that form the transmembrane channel and contain the substrate binding sites. Structural analyses have found a variety of seemingly unrelated folds for the ABC transporter transmembrane domains, and from these a set of diverse mechanistic models has been inferred. Nevertheless, in spite of the explosion in structure determination of ABC transporters in the last decade, advancement in certainty and clarity as to fundamental aspects of their molecular mechanisms remains elusive. With this in mind, here we put and examine the question: Could current ABC structures differ from the physiologic membrane-embedded forms?

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http://hdl.handle.net/10453/144788