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

Author:

Balakrishna Asha Manikkoth1,Seelert Holger2,Marx Sven-Hendric2,Dencher Norbert A.2,Grüber Gerhard1

Affiliation:

1. Nanyang Technological University, School of Biological Sciences, 60 Nanyang Drive, Singapore 637551, Republic of Singapore

2. Physikalische Biochemie, Fachbereich Chemie, Technische Universität Darmstadt, Alarich-Weiss-Str.4, D-64287 Darmstadt, Germany

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 β=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.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference42 articles.

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3. Crystallization of the c14-rotor of the chloroplast ATP synthase reveals that it contains pigments;Varco-Merth;Biochim. Biophys. Acta,2008

4. Structure at 2.8-angstom resolution of F1-ATPase from bovine heart-mitochondria;Abrahams;Nature,1994

5. ATP synthase: an electrochemical transducer with rotatory mechanics;Junge;TIBS,1997

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