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{Symersky:2012:10.1038/nsmb.2284,
author = {Symersky, J and Pagadala, V and Osowski, D and Krah, A and Meier, T and Faraldo-Gomez, JD and Mueller, DM},
doi = {10.1038/nsmb.2284},
journal = {Nature Structural and Molecular Biology},
pages = {485--491},
title = {Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation},
url = {http://dx.doi.org/10.1038/nsmb.2284},
volume = {19},
year = {2012}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - The proton pore of the F1Fo ATP synthase consists of a ring of c subunits, which rotates, driven by downhill proton diffusion across the membrane. An essential carboxylate side chain in each subunit provides a proton-binding site. In all the structures of c-rings reported to date, these sites are in a closed, ion-locked state. Structures are here presented of the c10 ring from Saccharomyces cerevisiae determined at pH 8.3, 6.1 and 5.5, at resolutions of 2.0 Å, 2.5 Å and 2.0 Å, respectively. The overall structure of this mitochondrial c-ring is similar to known homologs, except that the essential carboxylate, Glu59, adopts an open extended conformation. Molecular dynamics simulations reveal that opening of the essential carboxylate is a consequence of the amphiphilic nature of the crystallization buffer. We propose that this new structure represents the functionally open form of the c subunit, which facilitates proton loading and release.
AU - Symersky,J
AU - Pagadala,V
AU - Osowski,D
AU - Krah,A
AU - Meier,T
AU - Faraldo-Gomez,JD
AU - Mueller,DM
DO - 10.1038/nsmb.2284
EP - 491
PY - 2012///
SN - 1545-9985
SP - 485
TI - Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation
T2 - Nature Structural and Molecular Biology
UR - http://dx.doi.org/10.1038/nsmb.2284
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000303611200005&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - https://www.nature.com/articles/nsmb.2284
UR - http://hdl.handle.net/10044/1/94603
VL - 19
ER -