P1BPUMPS

Structural and functional characterization of molecular nanomachines: principles of transition metal selectivity and transport in heavy metal P1B-type ATPases

Coordinatore	AARHUS UNIVERSITET    more  Organization address address: Nordre Ringgade 1 city: AARHUS C postcode: 8000 contact info Titolo: Ms. Nome: Lene Cognome: Hogenhof Kristensen Email: send email Telefono: +45 8942 5058 Fax: +45 8612 3178
Nazionalità Coordinatore	Denmark [DK]
Totale costo	278˙903 €
EC contributo	278˙903 €
Programma	FP7-PEOPLE Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013)
Code Call	FP7-PEOPLE-2009-IOF
Funding Scheme	MC-IOF
Anno di inizio	2011
Periodo (anno-mese-giorno)	2011-03-01   -   2014-02-28

 Partecipanti

#	participant	country	role	EC contrib. [€]
1	AARHUS UNIVERSITET  Organization address address: Nordre Ringgade 1 city: AARHUS C postcode: 8000 contact info Titolo: Ms. Nome: Lene Cognome: Hogenhof Kristensen Email: send email Telefono: +45 8942 5058 Fax: +45 8612 3178	DK (AARHUS C)	coordinator	278˙903.10

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 Obiettivo del progetto (Objective)

'Cellular concentrations of transition metals are tightly regulated to a necessary balance to satisfy essential requirements for the activity of fundamental biochemical processes and avoid toxic levels which would impair cell survival. P1B-type ATPases are a family of membrane ion pumps which utilize the energy generated by ATP hydrolysis to drive the selective heavy metal translocation across the cellular membrane against the electrochemical gradient. Although playing a pivotal role in regulating the concentrations of essential physiological metal elements (e.g: Cu, Zn) and toxic transition metals (e.g.: Cd, Pb), the mechanism by which these molecular machines perform their function are not understood in detail. The proposed project aims to reveal at a molecular level the principles and determinants for heavy metal selectivity, metal binding geometry, metal translocation pathway, and energy transduction processes in energy-driven metal transport in P1B-type ATPases. A complementary X-ray crystallographic and biochemical approach will be developed in order to obtain a molecular understanding of the three-dimensional structure and the function of prokaryotic P1B-type ATPases. The final goal is to reveal how these molecular machines convert the energy stored in ATP into conformational changes which result into directional transport of heavy metal across the lipid bilayer. Elucidating the mechanism of transition metal transport across biological membranes accomplished by P1B-type ATPases will shed light on an essential biochemical process conserved in all the kingdoms of life and will provide the bases for the future rational design of modulators of P1B-type ATPase activity.'