2W5J

Structure of the c14-rotor ring of the proton translocating chloroplast ATP synthase

Summary for 2W5J

• Entry DOI: 10.2210/pdb2w5j/pdb
• Descriptor: ATP SYNTHASE C CHAIN, CHLOROPLASTIC (1 entity in total)
• Functional Keywords: hydrolase, chloroplast, atp synthase, lipid-binding, cf(0), membrane, transport, formylation, energy transduction, hydrogen ion transport, ion transport, transmembrane, membrane protein
• Biological source: SPINACIA OLERACEA (SPINACH)
• Cellular location: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein: P69447
• Total number of polymer chains: 14
• Total formula weight: 106398.11

Authors

Vollmar, M.,Schlieper, D.,Winn, M.,Buechner, C.,Groth, G. (deposition date: 2008-12-10, release date: 2009-05-19, Last modification date: 2023-12-13)

Primary citation

Vollmar, M.,Schlieper, D.,Winn, M.,Buchner, C.,Groth, G.
Structure of the c14 rotor ring of the proton translocating chloroplast ATP synthase.
J. Biol. Chem., 284:18228-18235, 2009

PubMed Abstract: The structure of the membrane integral rotor ring of the proton translocating F(1)F(0) ATP synthase from spinach chloroplasts was determined to 3.8 A resolution by x-ray crystallography. The rotor ring consists of 14 identical protomers that are symmetrically arranged around a central pore. Comparisons with the c(11) rotor ring of the sodium translocating ATPase from Ilyobacter tartaricus show that the conserved carboxylates involved in proton or sodium transport, respectively, are 10.6-10.8 A apart in both c ring rotors. This finding suggests that both ATPases have the same gear distance despite their different stoichiometries. The putative proton-binding site at the conserved carboxylate Glu(61) in the chloroplast ATP synthase differs from the sodium-binding site in Ilyobacter. Residues adjacent to the conserved carboxylate show increased hydrophobicity and reduced hydrogen bonding. The crystal structure reflects the protonated form of the chloroplast c ring rotor. We propose that upon deprotonation, the conformation of Glu(61) is changed to another rotamer and becomes fully exposed to the periphery of the ring. Reprotonation of Glu(61) by a conserved arginine in the adjacent a subunit returns the carboxylate to its initial conformation.

PubMed: 19423706
DOI: 10.1074/jbc.M109.006916

Experimental method

X-RAY DIFFRACTION (3.8 Å)