Summary
The proton ATP synthase consists of a membrane integratedpart, Fo, and a hydrophilic part, F1. F1. is composed of five different subunits: α, β, γ δ, and ε. This chapter focuses on the chloroplast F1 (CF1) structure and discusses the overall shape and dimensions of CF1, shape and size of the various subunits, subunit interactions and conformational changes in the subunit positions related to catalysis. Structural data originate mainly from X-ray diffraction and electron microscopy. Recently, the structure of F1 from beef heart mitochondria has been determined at 2.8 Å and this structure, although not fully identical to CF1, can be taken as a blueprint for models of the CF1 structure.
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References
Abrahams JP, Lutter R, Todd RJ, van Raaij MJ, Leslie AGW and Walker JE (1993) Inherent asymmetry of the structure of F1-ATPase from bovine heart mitochondria at 6.5 Å resolution. EMBO J 12: 1775–1780
Abrahams JP, Leslie AGW, Lutter R and Walker JE (1994) Structure at 2.8 Á resolution of F1-ATPase from bovine heart mitochondria. Nature 370: 621–628
Beckers G, Berzborn RJ and Strotmann H (1992) Zero-length crosslinking between subunits δ and I of the H+-translocating ATPase of chloroplasts. Biochim Biophys Acta 1101: 97–104
Banchet M, Ysern X, Hullihen J, Pedersen PL and Amzel, LM (1991) Mitochondrial ATP synthase. Quaternary structure of the F1 moiety at 3.6 Å determined by X-ray diffraction. J Biol Chem 266: 21197–21201
Boekema EJ and Böttcher B (1992) The structure of ATP synthase from chloroplasts. Conformational changes of CF1 studied by electron microscopy. Biochim Biophys Acta 1098: 131–143
Boekema EJ, Berden JA, and van Heel MG (1986) Structure of mitochondrial F1-ATPase studied by electron microscopy and image processing. Biochim Biophys Acta 851: 353–360
Boekema E J, Schmidt G, Gräber P and Berden JA (1988) Structure of the ATP-synthase from chloroplasts and mitochondria by electron microscopy. Zeitschrift Naturforsch. 43c: 219–225
Boekema EJ, Xiao J, and McCarty RE (1990) Structure of the ATP synthase from chloroplasts studied by electron microscopy. Localization of the small subunits. Biochim Biophys Acta 1020: 49–56
Boekema EJ, Harris D, Böttcher B and Gräber P (1992) The structure of the ATP-synthase from chloroplasts. In: Murata N (ed) Research in Photosynthesis, Vol 2, pp 645–652. Kluwer Academic Publishers, Dordrecht
Codd R, Cox G, Guss JM, Solomon RG and Webb D (1992) The expression, purification and crystallization of the ε subunit of the F1 portion of the ATPase of Escherichia coli. J Mol Biol 228: 306–309
Cox GB, Cromer BA, Guss JM, Harvey, I, Jeffrey PD, Solomon RG and Webb DC (1993) Formation in vivo, purification and crystallization of a complex of the γ and ε subunits of the FoF1-ATPase of Escherichia coli. J Mol Biol 229: 1159–1162
Dunn SD (1982) The isolated γ subunit of Escherichia coli F1 ATPase binds the ε subunit. J Biol Chem 257: 7354–7359
Engelbrecht S and Junge W (1990) Subunit δ of H+-ATPase At the interface between proton flow and ATP synthesis. Biochim Biophys Acta 1015: 379–390
Gogol EP, Lücken U, Bork T and Capaldi RA (1989a) Molecular architecture of Escherichia coli F1 adenosinetriphosphatase. Biochemistry 28: 4709–4716
Gogol EP, Aggeler R, Sagermann M and Capaldi RA (1989b) Cryoelectron microscopy of Escherichia coli F1 adenosinetriphosphatase decorated with monoclonal antibodies to individual subumits of the complex. Biochemistry 28: 4717–4724.
Gogol EP, Johnston E, Aggeler R and Capaldi RA (1990) Ligand-dependent structural variations in Escherichiacoli F1 ATPase revealed by cryoelectron microscopy. Proc Natl Acad Sci USA 87: 9585–9589
Hoesche JA and Berzborn R (1993) Primary structure, deduced from cDNA, secondary structure analysis and conclusions concerning interaction surfaces of the δ subunit of the photosynthetic ATP-synthase (E.C. 3.6.1.34) from millet (Sorghum bicolor) and maize (Zea mays). Biochim Biophys Acta 1142: 293–305
Ishii N, Yoshimura H, Nagayama K, Kagawa Y and Yoshida M (1993) Three-dimensional structure of F1-ATPase of thermophilic bacterium PS3 obtained by electron crystallography. J Biochem 113: 245–250
Lücken U, Gogol EP and Capaldi RA (1990) Structure of the ATP synthase complex (ECF1Fo) of Escherichia coli from cryoelectron microscopy. Biochemistry 29: 5339–5343
McCarty, RE and Hammes GG (1987) Molecular architecture of chloroplast coupling factor 1. Trends Biol Sci 12: 234–237
Tozawa K, Miyauchi M and Yoshida M (1993) Structure of the α subunit of F1-ATPase probed by limited proteolysis. J Biol Chem 268: 19044–19054
Wagner R, Apley EC, Engelbrecht S and Junge W (1988) The binding of eosin-labeled subunit δ to the isolated chloroplast ATPase, CF1, as revealed by rotational diffusion in solution. FEBS Lett 230: 109–115
Wang Z-Y, Freire E and McCarty RE (1993) Influence of nucleotide binding site occupancy on the thermal stability of the F1 portion of the chloroplast ATP synthase. J Biol Chem 268: 20785–20790
Wilkens S and Capaldi RA (1992) Monomaleimidogold labeling of the γ subunit of the Escherichia coli F1 ATPase examined by cryoelectron microscopy. Arch Biochem Biophys 299: 105–109
Wilkens S and Capaldi RA (1994) Asymmetry and structural changes in ECF1 examined by cryoelectronmicroscopy. Biol Chem Hoppe-Seyler 375: 43–51
Wilkens S, Dunn SD and Capaldi RA (1994) A cryoelectron microscopy study of the interaction of the Escherichia coli F1-ATPase with subunit β dimer. FEBS Lett. 354: 37–40
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© 1996 Kluwer Academic Publishers
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Boekema, E.J., Lücken, U. (1996). The Structure of the CF1 Part of the ATP-Synthase Complex from Chloroplasts. In: Ort, D.R., Yocum, C.F., Heichel, I.F. (eds) Oxygenic Photosynthesis: The Light Reactions. Advances in Photosynthesis and Respiration, vol 4. Springer, Dordrecht. https://doi.org/10.1007/0-306-48127-8_26
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DOI: https://doi.org/10.1007/0-306-48127-8_26
Publisher Name: Springer, Dordrecht
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