Gutenberg Open Science: What monomeric nucleotide binding domains can teach us about dimeric ABC proteins

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-6132

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DC Field	Value	Language
dc.contributor.author	Ford, Robert C.	-
dc.contributor.author	Hellmich, Ute A.	-
dc.date.accessioned	2021-06-29T08:20:54Z	-
dc.date.available	2021-06-29T08:20:54Z	-
dc.date.issued	2020	-
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/6141	-
dc.description.abstract	The classic conceptualization of ATP binding cassette (ABC) transporter function is an ATP-dependent conformational change coupled to transport of a substrate across a biological membrane via the transmembrane domains (TMDs). The binding of two ATP molecules within the transporter's two nucleotide binding domains (NBDs) induces their dimerization. Despite retaining the ability to bind nucleotides, isolated NBDs frequently fail to dimerize. ABC proteins without a TMD, for example ABCE and ABCF, have NBDs tethered via elaborate linkers, further supporting that NBD dimerization does not readily occur for isolated NBDs. Intriguingly, even in full-length transporters, the NBD-dimerized, outward-facing state is not as frequently observed as might be expected. This leads to questions regarding what drives NBD interaction and the role of the TMDs or linkers. Understanding the NBD–nucleotide interaction and the subsequent NBD dimerization is thus pivotal for understanding ABC transporter activity in general. Here, we hope to provide new insights into ABC protein function by discussing the perplexing issue of (missing) NBD dimerization in isolation and in the context of full-length ABC proteins.	en_GB
dc.language.iso	eng	de
dc.rights	CC BY-NC-ND	*
dc.rights.uri	https://creativecommons.org/licenses/by-nc-nd/4.0/	*
dc.subject.ddc	540 Chemie	de_DE
dc.subject.ddc	540 Chemistry and allied sciences	en_GB
dc.title	What monomeric nucleotide binding domains can teach us about dimeric ABC proteins	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-6132	-
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 09 Chemie, Pharmazie u. Geowissensch.	de
jgu.organisation.number	7950	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	FEBS letters	de
jgu.journal.volume	594	de
jgu.journal.issue	23	de
jgu.pages.start	3857	de
jgu.pages.end	3875	de
jgu.publisher.year	2020	-
jgu.publisher.name	Wiley	de
jgu.publisher.place	Chichester	de
jgu.publisher.uri	https://doi.org/10.1002/1873-3468.13921	de
jgu.publisher.issn	1873-3468	de
jgu.organisation.place	Mainz	-
jgu.subject.ddccode	540	de
jgu.publisher.doi	10.1002/1873-3468.13921
jgu.organisation.ror	https://ror.org/023b0x485
Appears in collections:	JGU-Publikationen

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