Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050307 | FEBS Letters | 2006 | 7 Pages |
Abstract
The F1F0 ATP synthase has been purified from the hyperthermophilic eubacterium Aquifex aeolicus and characterized. Its subunits have been identified by MALDI-mass spectrometry through peptide mass fingerprinting and MS/MS. It contains the canonical subunits α, β, γ, δ and ε of F1 and subunits a and c of F0. Two versions of the b subunit were found, which show a low sequence homology to each other. Most likely they form a heterodimer. An electron microscopic single particle analysis revealed clear structural details, including two stalks connecting F1 and F0. In several orientations the central stalk appears to be tilted and/or kinked. It is unclear whether there is a direct connection between the peripheral stalk and the δ subunit.
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Authors
Guohong Peng, Mihnea Bostina, Michael Radermacher, Isam Rais, Michael Karas, Hartmut Michel,