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The structure of the F0F.1-ATPases
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The previously isolated F1-ATPases are all made up of five different subunits (α3, β3, γ1, δ1, ŋ1), each of which is on the right three, orange-shaped α- and β-subunits (UE), together with the stem-shaped γ-UE  are shown. The spherical arrangement of the α and β UE is approximately 100 Å in diameter. The structure of the two teaching units is very similar; the N-terminal domain is a 6-stranded β-barrel followed by one central nucleotide binding site consisting of 9 parallel β-sheets and 9 associated α-helices . The C-terminus consists of an α-helix bundle (7 helices in the α-UE, 6 helices in the β-UE).
The F1-ATPase appears to have the γ-UE  with the F0Component to be connected. The γ-UE can rotate because it has only a few points of contact with the αβ structure. One of these is at its extreme C-terminus. Amino acids 261-271 have hydrophobic side chains, which are formed by a shaft formed from 6 loops of the αβ-UE in the correct position  being held. This rotational movement is part of the molecular motor of the F.1-UE and causes the conformational change of the β-UE with the catalytic centers for the hydrolysis of ATP.
Both the α and β UE contain nucleotide binding sites. Although the β-UE has a nucleotide binding site, it has no bound nucleotide, which has a decisive influence on the conformation of this UE. The nucleotide-binding domain and the C-terminus rotate by up to 30 ° - this rotates the C-terminus from the axis of the αβ complex in the direction of the γ-UE and the β-sheets of the nucleotide binding site lose some hydrogen bonds (click here )
The nucleotide binding sites are at the contact points of the subunits - the binding of the nucleotides is influenced by the neighboring subunit. The three catalytic centers are also located in the three β-UE.