Project Details
Projekt
Crystallization and Structural Analysis of the ATP-Synthase (FoF1) from the thermophilic Cyanobacterium Synechococcus elongatus
Applicant
Professorin Dr. Petra Fromme
Subject Area
Biophysics
Term
from 1999 to 2004
Project identifier
Deutsche Forschungsgemeinschaft (DFG) - Project number 5172172
One of the most important proteins in energy transduction is the ATP-Synthase (FoF1). This membrane-bound enzyme complex is present in all living organisms. It catalyzes the synthesis of ATP from ADP and Pi, driven by a transmembrane electrochemical potential of protons or sodiumions. The enzyme complex consists of three distinct structural and functional domains: A membrane intrinsic proton translocation system (the Fo part) which is coupled to the membrane extrinsic domain (the F1 part), which in turn harbors the nucleotide binding sites, by at least two "stalks". The structure of the F1 part was solved by X-ray structure analysis in 1994 by Abrahams et al. [1], leading to the Novel price for J. Walker together with J.P. Boyer in 1997. They proposed a rotational binding change mechanism, but the molecular elucidation of the coupling mechanism suffers from the lack of information on the structure of the membrane intrinsic proton translocation machinery and the energy transducing stalk region of the protein complex. In this project we want to crystallize the complete intact FoF1, containing all three domains, from the thermophilic Cyanobacterium Synechococcus elongatus for X-ray structure analysis. The structure will be the basis for the determination of the proton translocating mechanism in Fo and the energy transduction to the catalytic cycle in the F1 part. [1] Abrahams, J.P., Leslie, A.G.W., Lutter R. and Walker, J.E. (1994) Nature 370, 621-628.
DFG Programme
Priority Programmes
