dc.contributor.author
Andersson, Magnus
dc.contributor.author
Bondar, Ana-Nicoleta
dc.contributor.author
Freites, J. Alfredo
dc.contributor.author
Tobias, Douglas J.
dc.contributor.author
Kaback, H. Ronald
dc.contributor.author
White, Stephen H.
dc.date.accessioned
2018-06-08T03:54:09Z
dc.date.available
2014-09-04T11:55:38.833Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/16178
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-20362
dc.description.abstract
Lactose permease of Escherichia coli (LacY) catalyzes symport of a
galactopyranoside and an H+ via an alternating access mechanism. The
transition from an inward- to an outward-facing conformation of LacY involves
sugar-release followed by deprotonation. Because the transition depends
intimately upon the dynamics of LacY in a bilayer environment, molecular
dynamics (MD) simulations may be the only means of following the accompanying
structural changes in atomic detail. Here, we describe MD simulations of wild-
type apo LacY in phosphatidylethanolamine (POPE) lipids that features two
protonation states of the critical Glu325. While the protonated system
displays configurational stability, deprotonation of Glu325 causes significant
structural rearrangements that bring into proximity side chains important for
H+ translocation and sugar binding and closes the internal cavity. Moreover,
protonated LacY in phosphatidylcholine (DMPC) lipids shows that the observed
dynamics are lipid-dependent. Together, the simulations describe early
dynamics of the inward-to-outward transition of LacY that agree well with
experimental data.
en
dc.rights.uri
http://www.elsevier.com/open-access/userlicense/1.0/
dc.subject.ddc
500 Naturwissenschaften und Mathematik::530 Physik
dc.title
Proton-coupled dynamics in lactose permease
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
Structure. - 20 (2012), 11, S. 1893-1904
dc.identifier.sepid
24841
dcterms.bibliographicCitation.doi
10.1016/j.str.2012.08.021
dcterms.bibliographicCitation.url
http://dx.doi.org/10.1016/j.str.2012.08.021
refubium.affiliation
Physik
de
refubium.affiliation.other
Institut für Theoretische Physik
refubium.mycore.fudocsId
FUDOCS_document_000000020893
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000003867
dcterms.accessRights.openaire
open access
dcterms.isPartOf.issn
09692126