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F-ATPase

Towards a Complete Quantitative Model of the FOF1 ATP Synthase

Total Cost €

EC-Contrib. €

Partnership

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Outcomes and
results

F-ATPase project word cloud

Explore the words cloud of the F-ATPase project. It provides you a very rough idea of what is the project "F-ATPase" about.

found nanomotor motor reverse complete description quantitative gradient rotary experiments coupled elucidated enzymatic abundantly catalytic separate lipid careful accounts cellular bilayers atp fof1 consists inorganic biochemical clever sparse absence nearly synthesis protons acts hydrolyzing camshaft proton describes exchange function inducing biophysical flow conformational f1 atpase cycle rotational pump thermodynamic respiration made integral fo membrane functional perform motors synthesizes portion converts relatively phosphate adp last interactions sites 90

Project "F-ATPase" data sheet

The following table provides information about the project.

Coordinator	MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV Organization address address: HOFGARTENSTRASSE 8 city: MUENCHEN postcode: 80539 website: n.a. contact info title: n.a. name: n.a. surname: n.a. function: n.a. email: n.a. telephone: n.a. fax: n.a.
Coordinator Country	Germany [DE]
Project website	http://www.mpibpc.mpg.de/15412994/ATPaseEnergyTransduction
Total cost	171˙460 €
EC max contribution	171˙460 € (100%)
Programme	1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
Code Call	H2020-MSCA-IF-2015
Funding Scheme	MSCA-IF-EF-ST
Starting year	2016
Duration (year-month-day)	from 2016-03-01 to 2018-02-28

Partnership

Take a look of project's partnership.

#	participants	country	role	EC contrib. [€]
1	MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV Organization address address: HOFGARTENSTRASSE 8 city: MUENCHEN postcode: 80539 website: n.a. contact info title: n.a. name: n.a. surname: n.a. function: n.a. email: n.a. telephone: n.a. fax: n.a.	DE (MUENCHEN)	coordinator	171˙460.00

Map

Project objective

The FOF1-ATPase is a complex nanomotor that synthesizes nearly 90% of the ATP made during cellular respiration. It consists of two coupled rotary motors: an integral membrane complex driven by proton flow across lipid bilayers (FO) and an enzymatic complex that converts ADP and inorganic phosphate to ATP (F1). The rotational portion of these motors acts as a camshaft, inducing conformational changes that lead to ATP synthesis in the F1 motor’s three functional catalytic sites. The F1 motor can perform ATP synthesis in the absence of FO, and it can also work in reverse, hydrolyzing ATP to pump protons against an established gradient. Over the last 30 years many important aspects of this motor’s function have been elucidated by careful biochemical work and further understood by clever biophysical experiments. However, there is still not a complete, quantitative description of the whole thermodynamic cycle—one that fully describes the interactions between all three separate catalytic sites and accounts for the need to exchange ATP (found abundantly) for the relatively sparse ADP.

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