ABCTRANSPORT

Minimalist multipurpose ATP-binding cassette transporters

Coordinatore	RIJKSUNIVERSITEIT GRONINGEN    more Spiacenti, non ci sono informazioni su questo coordinatore. Contattare Fabio per maggiori infomrazioni, grazie.
Nazionalità Coordinatore	Netherlands [NL]
Totale costo	1˙500˙000 €
EC contributo	1˙500˙000 €
Programma	FP7-IDEAS-ERC Specific programme: "Ideas" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
Code Call	ERC-2011-StG_20101109
Funding Scheme	ERC-SG
Anno di inizio	2012
Periodo (anno-mese-giorno)	2012-01-01   -   2016-12-31

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	RIJKSUNIVERSITEIT GRONINGEN  Organization address address: Broerstraat 5 city: GRONINGEN postcode: 9712CP contact info Titolo: Dr. Nome: Dick Cognome: Veldhuis Email: send email Telefono: +3150363 4142 Fax: +0031 50 363 4500	NL (GRONINGEN)	hostInstitution	1˙500˙000.00
2	RIJKSUNIVERSITEIT GRONINGEN  Organization address address: Broerstraat 5 city: GRONINGEN postcode: 9712CP contact info Titolo: Dr. Nome: Dirk Jan Cognome: Slotboom Email: send email Telefono: -3634206	NL (GRONINGEN)	hostInstitution	1˙500˙000.00

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 Obiettivo del progetto (Objective)

'Many Gram-positive (pathogenic) bacteria are dependent on the uptake of vitamins from the environment or from the infected host. We have recently discovered the long-elusive family of membrane protein complexes catalyzing such transport. The vitamin transporters have an unprecedented modular architecture consisting of a single multipurpose energizing module (the Energy Coupling Factor, ECF) and multiple exchangeable membrane proteins responsible for substrate recognition (S-components). The S-components have characteristics of ion-gradient driven transporters (secondary active transporters), whereas the energizing modules are related to ATP-binding cassette (ABC) transporters (primary active transporters).

The aim of the proposal is threefold: First, we will address the question how properties of primary and secondary transporters are combined in ECF transporters to obtain a novel transport mechanism. Second, we will study the fundamental and unresolved question how protein-protein recognition takes place in the hydrophobic environment of the lipid bilayer. The modular nature of the ECF proteins offers a natural system to study the driving forces used for membrane protein interaction. Third, we will assess whether the ECF transport systems could become targets for antibacterial drugs. ECF transporters are found exclusively in prokaryotes, and their activity is often essential for viability of Gram-positive pathogens. Thus they could turn out to be an Achilles’ heel for the organisms.

Structural and mechanistic studies (X-ray crystallography, microscopy, spectroscopy and biochemistry) will reveal how the different transport modes are combined in a single protein complex, how transport is energized and catalyzed, and how protein-protein recognition takes place. Microbiological screens will be developed to search for compounds that inhibit prokaryote-specific steps of the mechanism of ECF transporters.'