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Crystallographic structure of the turbine C-ring from spinach chloroplast F-ATP synthase.


ABSTRACT: In eukaryotic and prokaryotic cells, F-ATP synthases provide energy through the synthesis of ATP. The chloroplast F-ATP synthase (CF1FO-ATP synthase) of plants is integrated into the thylakoid membrane via its FO-domain subunits a, b, b' and c Subunit c with a stoichiometry of 14 and subunit a form the gate for H+-pumping, enabling the coupling of electrochemical energy with ATP synthesis in the F1 sector.Here we report the crystallization and structure determination of the c14-ring of subunit c of the CF1FO-ATP synthase from spinach chloroplasts. The crystals belonged to space group C2, with unit-cell parameters a=144.420, b=99.295, c=123.51 Å, and ?=104.34° and diffracted to 4.5 Å resolution. Each c-ring contains 14 monomers in the asymmetric unit. The length of the c-ring is 60.32 Å, with an outer ring diameter 52.30 Å and an inner ring width of 40 Å.

SUBMITTER: Balakrishna AM 

PROVIDER: S-EPMC3971453 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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Crystallographic structure of the turbine C-ring from spinach chloroplast F-ATP synthase.

Balakrishna Asha Manikkoth AM   Seelert Holger H   Marx Sven-Hendric SH   Dencher Norbert A NA   Grüber Gerhard G  

Bioscience reports 20140401 2


In eukaryotic and prokaryotic cells, F-ATP synthases provide energy through the synthesis of ATP. The chloroplast F-ATP synthase (CF<sub>1</sub>F<sub>O</sub>-ATP synthase) of plants is integrated into the thylakoid membrane via its F<sub>O</sub>-domain subunits a, b, b' and c Subunit c with a stoichiometry of 14 and subunit a form the gate for H<sup>+</sup>-pumping, enabling the coupling of electrochemical energy with ATP synthesis in the F<sub>1</sub> sector.Here we report the crystallization a  ...[more]

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