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Salt-bridge dynamics control substrate-induced conformational change in the membrane transporter GlpT
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för fysikalisk kemi, oorganisk kemi och strukturkemi.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för fysikalisk kemi, oorganisk kemi och strukturkemi.
Vise andre og tillknytning
2008 (engelsk)Inngår i: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 378, nr 4, s. 828-839Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Active transport of substrates across cytoplasmic membranes is of great physiological, medical and pharmaceutical importance. The glycerol-3-phosphate (G3P) transporter (GlpT) of the E. coli inner membrane is a secondary active antiporter from the ubiquitous major facilitator superfamily that couples the import of G3P to the efflux of inorganic phosphate (Pi) down its concentration gradient. Integrating information from a novel combination of structural, molecular dynamics simulations and biochemical studies, we identify the residues involved directly in binding of substrate to the inward-facing conformation of GlpT, thus defining the structural basis for the substrate-specificity of this transporter. The substrate binding mechanism involves protonation of a histidine residue at the binding site. Furthermore, our data suggest that the formation and breaking of inter- and intradomain salt bridges control the conformational change of the transporter that accompanies substrate translocation across the membrane. The mechanism we propose may be a paradigm for organophosphate:phosphate antiporters.

sted, utgiver, år, opplag, sider
2008. Vol. 378, nr 4, s. 828-839
Emneord [en]
antiporter; membrane transport; major facilitator superfamily; molecular dynamics simulations; secondary active transport
HSV kategori
Identifikatorer
URN: urn:nbn:se:su:diva-24727DOI: 10.1016/j.jmb.2008.03.029ISI: 000256180100006OAI: oai:DiVA.org:su-24727DiVA, id: diva2:198199
Tilgjengelig fra: 2008-02-27 Laget: 2008-02-27 Sist oppdatert: 2017-12-13bibliografisk kontrollert
Inngår i avhandling
1. Structural modeling of membrane transporter proteins
Åpne denne publikasjonen i ny fane eller vindu >>Structural modeling of membrane transporter proteins
2008 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

A fundamental process of all living organisms - the transport of molecules across cellular membranes through membrane transport proteins - is investigated.

After a brief review of general properties of biological membranes follows a recollection of the major methods of membrane transport that Nature utilizes (Chapter 1). This is followed by a description of important experimental (Chapter 2) and theoretical methods (Chapter 3) for structural studies of membrane proteins. The findings on membrane protein transport in papers I-IV are then summarized (Chapter 4) and important findings are discussed. The remaining text is a discussion on relevant theoretical and experimental methods.

sted, utgiver, år, opplag, sider
Stockholm: Institutionen för fysikalisk kemi, oorganisk kemi och strukturkemi, 2008. s. 148
Emneord
membrane protein structure, membrane protein crystallography, membrane protein structure modelling
HSV kategori
Forskningsprogram
strukturkemi
Identifikatorer
urn:nbn:se:su:diva-7402 (URN)978-91-7155-590-8 (ISBN)
Disputas
2008-03-19, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 12 A, Stockholm, 10:00
Opponent
Veileder
Tilgjengelig fra: 2008-02-27 Laget: 2008-02-27bibliografisk kontrollert

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