Biochemical and electron microscopic characterization of the F1F0 ATP synthase from the hyperthermophilic eubacterium Aquifex aeolicus.

Abstract:

:The F(1)F(0) 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 alpha, beta, gamma, delta and epsilon of F(1) and subunits a and c of F(0). 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 F(1) and F(0). 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 delta subunit.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Peng G,Bostina M,Radermacher M,Rais I,Karas M,Michel H

doi

10.1016/j.febslet.2006.09.062

subject

Has Abstract

pub_date

2006-10-30 00:00:00

pages

5934-40

issue

25

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)01184-7

journal_volume

580

pub_type

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