Imperial College London
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ProfessorThomasMeier

Faculty of Natural Sciences, Department 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:2018:10.1126/science.aat4318,
author = {Hahn, A and Vonck, J and Mills, D and Meier, TK and Kühlbrandt, W},
doi = {10.1126/science.aat4318},
journal = {Science},
title = {Structure, mechanism, and regulation of the chloroplast ATP synthase},
url = {http://dx.doi.org/10.1126/science.aat4318},
volume = {360},
year = {2018}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - INTRODUCTION:Green plant chloroplasts convert light into chemical energy, and adenosine triphosphate (ATP) generated by photosynthesis is the prime source of biologically useful energy on the planet. Plants produce ATP by the chloroplast F1Fo ATP synthase (cF1Fo), a macromolecular machine par excellence, driven by the electrochemical proton gradient across the photosynthetic membrane. It consists of 26 protein subunits, 17 of them wholly or partly membrane-embedded. ATP synthesis in the hydrophilic α3β3 head (cF1) is powered by the cFo rotary motor in the membrane. cFo contains a rotor ring of 14 c subunits, each with a conserved protonatable glutamate. Subunit a conducts the protons to and from the c-ring protonation sites. The central stalk of subunits γ and ε transmits the torque from the Fo motor to the catalytic cF1 head, resulting in the synthesis of three ATP per revolution. The peripheral stalk subunits b, b′, and δ act as a stator to prevent unproductive rotation of cF1 with cFo.All rotary ATP synthases are, in principle, fully reversible. To prevent wasteful ATP hydrolysis, cF1Fo has a redox switch that inhibits adenosine triphosphatase (ATPase) activity in the dark.RATIONALE:Understanding the molecular mechanisms of this elaborate nanomachine requires detailed structures of the whole complex, ideally at atomic resolution. Because of the dynamic nature of this membrane protein complex, crystallization has been difficult and no high-resolution structure of an entire, functional ATP synthase is available. We reconstituted cF1Fo from spinach chloroplasts into lipid nanodiscs and determined its structure by cryo–electron microscopy (cryo-EM). Cryo-EM is the ideal technique for this study because it can deliver high-resolution structures of large, dynamic macromolecular assemblies that adopt a mixture of conformational states.RESULTS:We present the cryo-EM structure of the intact cF1Fo ATP synthase in lipid nanodiscs a
AU  - Hahn,A
AU  - Vonck,J
AU  - Mills,D
AU  - Meier,TK
AU  - Kühlbrandt,W
DO  - 10.1126/science.aat4318
PY  - 2018///
SN  - 0036-8075
TI  - Structure, mechanism, and regulation of the chloroplast ATP synthase
T2  - Science
UR  - http://dx.doi.org/10.1126/science.aat4318
UR  - http://hdl.handle.net/10044/1/59083
VL  - 360
ER  -
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