Abstract:
:Membrane transporters actively translocate their substrate by undergoing large-scale structural transitions between inward- (IF) and outward-facing (OF) states ('alternating-access' mechanism). Despite extensive structural studies, atomic-level mechanistic details of such structural transitions, and as importantly, their coupling to chemical events supplying the energy, remain amongst the most elusive aspects of the function of these proteins. Here we present a quantitative, atomic-level description of the functional thermodynamic cycle for the glycerol-3-phosphate:phosphate antiporter GlpT by using a novel approach in reconstructing the free energy landscape governing the IF↔OF transition along a cyclic transition pathway involving both apo and substrate-bound states. Our results provide a fully atomic description of the complete transport process, offering a structural model for the alternating-access mechanism and substantiating the close coupling between global structural transitions and local chemical events.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Moradi M,Enkavi G,Tajkhorshid Edoi
10.1038/ncomms9393subject
Has Abstractpub_date
2015-09-29 00:00:00pages
8393issn
2041-1723pii
ncomms9393journal_volume
6pub_type
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