Cryo-EM structure of the entire mammalian F-type ATP synthase

J 2020

Cryo-EM structure of the entire mammalian F-type ATP synthase

PINKE, G., L. ZHOU a L.A. SAZANOV

Základní údaje

Originální název

Cryo-EM structure of the entire mammalian F-type ATP synthase

Autoři

PINKE, G., L. ZHOU a L.A. SAZANOV

Vydání

NATURE STRUCTURAL & MOLECULAR BIOLOGY, NEW YORK, NATURE PUBLISHING GROUP, 2020, 1545-9993

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 15.369

Kód RIV

RIV/00216224:14740/20:00121456

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1038/s41594-020-0503-8

UT WoS

000569299400004

Klíčová slova anglicky

MITOCHONDRIAL PERMEABILITY TRANSITION; C-SUBUNIT; COMPLEX I; ATOMIC MODEL; ARCHITECTURE; PREDICTION; CHANNEL; REGION; DIMERS; MOTION

Štítky

ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 29. 4. 2021 12:26, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

The majority of adenosine triphosphate (ATP) powering cellular processes in eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo, determined by cryo-electron microscopy. Subunits in the membrane domain are arranged in the 'proton translocation cluster' attached to the c-ring and a more distant 'hook apparatus' holding subunit e. Unexpectedly, this subunit is anchored to a lipid 'plug' capping the c-ring. We present a detailed proton translocation pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled c-ring, suggesting permeability transition pore opening. We propose a model for the permeability transition pore opening, whereby subunit e pulls the lipid plug out of the c-ring. Our structure will allow the design of drugs for many emerging applications in medicine. Cryo-EM structures of the entire mammalian F1Fo ATPase reveal several new features and details on the proton translocation pathway and suggest a model for the opening of the permeability transition pore.

Návaznosti

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

PINKE, G., L. ZHOU a L.A. SAZANOV. Cryo-EM structure of the entire mammalian F-type ATP synthase. NATURE STRUCTURAL & MOLECULAR BIOLOGY. NEW YORK: NATURE PUBLISHING GROUP, 2020, roč. 27, č. 11, s. 1077-1101. ISSN 1545-9993. Dostupné z: https://dx.doi.org/10.1038/s41594-020-0503-8.

@article{1762522,
   author = {Pinke, G. and Zhou, L. and Sazanov, L.A.},
   article_location = {NEW YORK},
   article_number = {11},
   doi = {http://dx.doi.org/10.1038/s41594-020-0503-8},
   keywords = {MITOCHONDRIAL PERMEABILITY TRANSITION; C-SUBUNIT; COMPLEX I; ATOMIC MODEL; ARCHITECTURE; PREDICTION; CHANNEL; REGION; DIMERS; MOTION},
   language = {eng},
   issn = {1545-9993},
   journal = {NATURE STRUCTURAL & MOLECULAR BIOLOGY},
   title = {Cryo-EM structure of the entire mammalian F-type ATP synthase},
   url = {https://www.nature.com/articles/s41594-020-0503-8},
   volume = {27},
   year = {2020}
}

TY  - JOUR
ID  - 1762522
AU  - Pinke, G. - Zhou, L. - Sazanov, L.A.
PY  - 2020
TI  - Cryo-EM structure of the entire mammalian F-type ATP synthase
JF  - NATURE STRUCTURAL & MOLECULAR BIOLOGY
VL  - 27
IS  - 11
SP  - 1077
EP  - 1077
PB  - NATURE PUBLISHING GROUP
SN  - 15459993
KW  - MITOCHONDRIAL PERMEABILITY TRANSITION
KW  - C-SUBUNIT
KW  - COMPLEX I
KW  - ATOMIC MODEL
KW  - ARCHITECTURE
KW  - PREDICTION
KW  - CHANNEL
KW  - REGION
KW  - DIMERS
KW  - MOTION
UR  - https://www.nature.com/articles/s41594-020-0503-8
N2  - The majority of adenosine triphosphate (ATP) powering cellular processes in eukaryotes is produced by the mitochondrial F1Fo ATP synthase. Here, we present the atomic models of the membrane Fo domain and the entire mammalian (ovine) F1Fo, determined by cryo-electron microscopy. Subunits in the membrane domain are arranged in the 'proton translocation cluster' attached to the c-ring and a more distant 'hook apparatus' holding subunit e. Unexpectedly, this subunit is anchored to a lipid 'plug' capping the c-ring. We present a detailed proton translocation pathway in mammalian Fo and key inter-monomer contacts in F1Fo multimers. Cryo-EM maps of F1Fo exposed to calcium reveal a retracted subunit e and a disassembled c-ring, suggesting permeability transition pore opening. We propose a model for the permeability transition pore opening, whereby subunit e pulls the lipid plug out of the c-ring. Our structure will allow the design of drugs for many emerging applications in medicine. Cryo-EM structures of the entire mammalian F1Fo ATPase reveal several new features and details on the proton translocation pathway and suggest a model for the opening of the permeability transition pore.
ER  -

PINKE, G., L. ZHOU a L.A. SAZANOV. Cryo-EM structure of the entire mammalian F-type ATP synthase. \textit{NATURE STRUCTURAL \&{}amp; MOLECULAR BIOLOGY}. NEW YORK: NATURE PUBLISHING GROUP, 2020, roč.~27, č.~11, s.~1077-1101. ISSN~1545-9993. Dostupné z: https://dx.doi.org/10.1038/s41594-020-0503-8.

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