Imperial College London

ProfessorThomasMeier

Faculty of Natural SciencesDepartment of Life Sciences

Visiting Professor
 
 
 
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Contact

 

t.meier Website

 
 
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Location

 

501Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Hahn:2016:10.1016/j.molcel.2016.05.037,
author = {Hahn, A and Parey, K and Bublitz, M and Mills, DJ and Zickermann, V and Vonck, J and Kühlbrandt, W and Meier, T},
doi = {10.1016/j.molcel.2016.05.037},
journal = {Molecular Cell},
pages = {445--456},
title = {Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology},
url = {http://dx.doi.org/10.1016/j.molcel.2016.05.037},
volume = {63},
year = {2016}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - We determined the structure of a complete, dimeric F1Fo-ATP synthase from yeast Yarrowia lipolytica mitochondria by a combination of cryo-EM and X-ray crystallography. The final structure resolves 58 of the 60 dimer subunits. Horizontal helices of subunit a in Fo wrap around the c-ring rotor, and a total of six vertical helices assigned to subunits a, b, f, i, and 8 span the membrane. Subunit 8 (A6L in human) is an evolutionary derivative of the bacterial b subunit. On the lumenal membrane surface, subunit f establishes direct contact between the two monomers. Comparison with a cryo-EM map of the F1Fo monomer identifies subunits e and g at the lateral dimer interface. They do not form dimer contacts but enable dimer formation by inducing a strong membrane curvature of ∼100°. Our structure explains the structural basis of cristae formation in mitochondria, a landmark signature of eukaryotic cell morphology.
AU - Hahn,A
AU - Parey,K
AU - Bublitz,M
AU - Mills,DJ
AU - Zickermann,V
AU - Vonck,J
AU - Kühlbrandt,W
AU - Meier,T
DO - 10.1016/j.molcel.2016.05.037
EP - 456
PY - 2016///
SN - 1097-4164
SP - 445
TI - Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology
T2 - Molecular Cell
UR - http://dx.doi.org/10.1016/j.molcel.2016.05.037
UR - http://hdl.handle.net/10044/1/33428
VL - 63
ER -