Details
| Original language | English |
|---|---|
| Pages (from-to) | 5769-5772 |
| Number of pages | 4 |
| Journal | FEBS letters |
| Volume | 579 |
| Issue number | 25 |
| Publication status | Published - 6 Oct 2005 |
Abstract
Respiration in all cells depends upon synthesis of ATP by the ATP synthase complex, a rotary motor enzyme. The structure of the catalytic moiety of ATP synthase, the so-called F1 headpiece, is well established. F 1 is connected to the membrane-bound and ion translocating F 0 subcomplex by a central stalk. A peripheral stalk, or stator, prevents futile rotation of the headpiece during catalysis. Although the enzyme functions as a monomer, several lines of evidence have recently suggested that monomeric ATP synthase complexes might interact to form a dimeric supercomplex in mitochondria. However, due to its fragility, the structure of ATP synthase dimers has so far not been precisely defined for any organism. Here we report the purification of a stable dimeric ATP synthase supercomplex, using mitochondria of the alga Polytomella. Structural analysis by electron microscopy and single particle analysis revealed that dimer formation is based on specific interaction of the F0 parts, not the F1 headpieces which are not at all in close proximity. Remarkably, the angle between the two F 0 part is about 70°, which induces a strong local bending of the membrane. Hence, the function of ATP synthase dimerisation is to control the unique architecture of the mitochondrial inner membrane.
Keywords
- ATP synthase, Dimer, Electron microscopy, Polytomella
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biophysics
- Biochemistry, Genetics and Molecular Biology(all)
- Structural Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
- Biochemistry, Genetics and Molecular Biology(all)
- Genetics
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology
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In: FEBS letters, Vol. 579, No. 25, 06.10.2005, p. 5769-5772.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Structure of dimeric ATP synthase from mitochondria
T2 - An angular association of monomers induces the strong curvature of the inner membrane
AU - Dudkina, Natalya V.
AU - Heinemeyer, Jesco
AU - Keegstra, Wilko
AU - Boekema, Egbert J.
AU - Braun, Hans Peter
N1 - Funding information: H.P.B. acknowledges a grant of the Deutsche Forschungsgemeinschaft (Br1829-7/1) and E.J.B. a grant of the Dutch science foundation NWO-CW.
PY - 2005/10/6
Y1 - 2005/10/6
N2 - Respiration in all cells depends upon synthesis of ATP by the ATP synthase complex, a rotary motor enzyme. The structure of the catalytic moiety of ATP synthase, the so-called F1 headpiece, is well established. F 1 is connected to the membrane-bound and ion translocating F 0 subcomplex by a central stalk. A peripheral stalk, or stator, prevents futile rotation of the headpiece during catalysis. Although the enzyme functions as a monomer, several lines of evidence have recently suggested that monomeric ATP synthase complexes might interact to form a dimeric supercomplex in mitochondria. However, due to its fragility, the structure of ATP synthase dimers has so far not been precisely defined for any organism. Here we report the purification of a stable dimeric ATP synthase supercomplex, using mitochondria of the alga Polytomella. Structural analysis by electron microscopy and single particle analysis revealed that dimer formation is based on specific interaction of the F0 parts, not the F1 headpieces which are not at all in close proximity. Remarkably, the angle between the two F 0 part is about 70°, which induces a strong local bending of the membrane. Hence, the function of ATP synthase dimerisation is to control the unique architecture of the mitochondrial inner membrane.
AB - Respiration in all cells depends upon synthesis of ATP by the ATP synthase complex, a rotary motor enzyme. The structure of the catalytic moiety of ATP synthase, the so-called F1 headpiece, is well established. F 1 is connected to the membrane-bound and ion translocating F 0 subcomplex by a central stalk. A peripheral stalk, or stator, prevents futile rotation of the headpiece during catalysis. Although the enzyme functions as a monomer, several lines of evidence have recently suggested that monomeric ATP synthase complexes might interact to form a dimeric supercomplex in mitochondria. However, due to its fragility, the structure of ATP synthase dimers has so far not been precisely defined for any organism. Here we report the purification of a stable dimeric ATP synthase supercomplex, using mitochondria of the alga Polytomella. Structural analysis by electron microscopy and single particle analysis revealed that dimer formation is based on specific interaction of the F0 parts, not the F1 headpieces which are not at all in close proximity. Remarkably, the angle between the two F 0 part is about 70°, which induces a strong local bending of the membrane. Hence, the function of ATP synthase dimerisation is to control the unique architecture of the mitochondrial inner membrane.
KW - ATP synthase
KW - Dimer
KW - Electron microscopy
KW - Polytomella
UR - http://www.scopus.com/inward/record.url?scp=26844548023&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2005.09.065
DO - 10.1016/j.febslet.2005.09.065
M3 - Article
C2 - 16223490
AN - SCOPUS:26844548023
VL - 579
SP - 5769
EP - 5772
JO - FEBS letters
JF - FEBS letters
SN - 0014-5793
IS - 25
ER -