Crossref
journal-article
Springer Science and Business Media LLC
Nature (297)
References
45
Referenced
239
-
Pogoryelov, D. et al. Engineering rotor ring stoichiometries in ATP synthases. Proc. Natl Acad. Sci. USA 109, E1599–E1608 (2012)
(
10.1073/pnas.1120027109
) / Proc. Natl Acad. Sci. USA by D Pogoryelov (2012) -
Abrahams, J. P., Leslie, A. G., Lutter, R. & Walker, J. E. Structure at 2.8 Å resolution of F1 ATPase from bovine heart mitochondria. Nature 370, 621–628 (1994)
(
10.1038/370621a0
) / Nature by JP Abrahams (1994) -
Davies, K. M. et al. Macromolecular organization of ATP synthase and complex I in whole mitochondria. Proc. Natl Acad. Sci. USA 108, 14121–14126 (2011)
(
10.1073/pnas.1103621108
) / Proc. Natl Acad. Sci. USA by KM Davies (2011) -
Mitome, N. et al. Essential arginine residue of the Fo-a subunit in FoF1-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the Fo proton channel. Biochem. J. 430, 171–177 (2010)
(
10.1042/BJ20100621
) / Biochem. J. by N Mitome (2010) - Cain, B. D. & Simoni, R. D. Interaction between Glu-219 and His-245 within the a-subunit of F1Fo-ATPase in Escherichia coli. J. Biol. Chem. 263, 6602–6612 (1988) / J. Biol. Chem. by BD Cain (1988)
-
van Lis, R., Mendoza-Hernández, G., Groth, G. & Atteia, A. New insights into the unique structure of the F0F1-ATP synthase from the chlamydomonad algae Polytomella sp. and Chlamydomonas reinhardtii. Plant Physiol. 144, 1190–1199 (2007)
(
10.1104/pp.106.094060
) / Plant Physiol. by R van Lis (2007) -
Symersky, J. et al. Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation. Nature Struct. Mol. Biol. 19, 485–491 (2012)
(
10.1038/nsmb.2284
) / Nature Struct. Mol. Biol. by J Symersky (2012) -
Rees, D. M., Leslie, A. G. & Walker, J. E. The structure of the membrane extrinsic region of bovine ATP synthase. Proc. Natl Acad. Sci. USA 106, 21597–21601 (2009)
(
10.1073/pnas.0910365106
) / Proc. Natl Acad. Sci. USA by DM Rees (2009) -
Andrade, M. A., Petosa, C., O’Donoghue, S. I., Muller, C. W. & Bork, P. Comparison of ARM and HEAT protein repeats. J. Mol. Biol. 309, 1–18 (2001)
(
10.1006/jmbi.2001.4624
) / J. Mol. Biol. by MA Andrade (2001) -
Jiang, W. & Fillingame, R. H. Interacting helical faces of subunits a and c in the F1F0 ATP synthase of Escherichia coli defined by disulfide cross-linking. Proc. Natl Acad. Sci. USA 95, 6607–6612 (1998)
(
10.1073/pnas.95.12.6607
) / Proc. Natl Acad. Sci. USA by W Jiang (1998) -
Moore, K. J. & Fillingame, R. H. Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase. J. Biol. Chem. 283, 31726–31735 (2008)
(
10.1074/jbc.M803848200
) / J. Biol. Chem. by KJ Moore (2008) -
Hakulinen, J. K. et al. A structural study on the architecture of the bacterial ATP synthase Fo motor. Proc. Natl Acad. Sci. USA 109, E2050–E2056 (2012)
(
10.1073/pnas.1203971109
) / Proc. Natl Acad. Sci. USA by JK Hakulinen (2012) -
Lau, W. C. Y. & Rubinstein, J. L. Subnanometre-resolution structure of the intact Thermus thermophilus H+-driven ATP synthase. Nature 481, 214–218 (2012)
(
10.1038/nature10699
) / Nature by WCY Lau (2012) -
Schwem, B. E. & Fillingame, R. H. Cross-linking between helices within subunit a of Escherichia coli ATP synthase defines the transmembrane packing of a four-helix bundle. J. Biol. Chem. 281, 37861–37867 (2006)
(
10.1074/jbc.M607453200
) / J. Biol. Chem. by BE Schwem (2006) -
Senes, A., Engel, D. E. & DeGrado, W. F. Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs. Curr. Opin. Struct. Biol. 14, 465–479 (2004)
(
10.1016/j.sbi.2004.07.007
) / Curr. Opin. Struct. Biol. by A Senes (2004) -
Hoppe, J., Schairer, H. U., Friedl, P. & Sebald, W. An Asp-Asn substitution in the proteolipid subunit of the ATP-synthase from Escherichia coli leads to a non-functional proton channel. FEBS Lett. 145, 21–29 (1982)
(
10.1016/0014-5793(82)81198-8
) / FEBS Lett. by J Hoppe (1982) -
Hatch, L. P., Cox, G. B. & Howitt, S. M. The essential arginine residue at position 210 in the a subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity. J. Biol. Chem. 270, 29407–29412 (1995)
(
10.1074/jbc.270.49.29407
) / J. Biol. Chem. by LP Hatch (1995) -
Angevine, C. A. & Fillingame, R. H. Aqueous access channels in subunit a of rotary ATP synthase. J. Biol. Chem. 278, 6066–6074 (2003)
(
10.1074/jbc.M210199200
) / J. Biol. Chem. by CA Angevine (2003) -
Pogoryelov, D. et al. Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases. Nature Chem. Biol. 6, 891–899 (2010)
(
10.1038/nchembio.457
) / Nature Chem. Biol. by D Pogoryelov (2010) -
Moore, K. J., Angevine, C. A., Vincent, O. D., Schwem, B. E. & Fillingame, R. H. The cytoplasmic loops of subunit a of Escherichia coli ATP synthase may participate in the proton translocating mechanism. J. Biol. Chem. 283, 13044–13052 (2008)
(
10.1074/jbc.M800900200
) / J. Biol. Chem. by KJ Moore (2008) -
Steed, P. R. & Fillingame, R. H. Residues in the polar loop of subunit c in Escherichia coli ATP synthase function in gating proton transport to the cytoplasm. J. Biol. Chem. 289, 2127–2138 (2014)
(
10.1074/jbc.M113.527879
) / J. Biol. Chem. by PR Steed (2014) -
Junge, W., Lill, H. & Engelbrecht, S. ATP synthase: an electrochemical transducer with rotatory mechanics. Trends Biochem. Sci. 22, 420–423 (1997)
(
10.1016/S0968-0004(97)01129-8
) / Trends Biochem. Sci. by W Junge (1997) -
Matthies, D. et al. High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na+-coupled ATP synthase. Nature Commun. 5,
http://dx.doi.org/10.1038/ncomms6286
(2014)
(
10.1038/ncomms6286
) -
van Lis, R., González-Halphen, D. & Atteia, A. Divergence of the mitochondrial electron transport chains from the green alga Chlamydomonas reinhardtii and its colorless close relative Polytomella. Biochim. Biophys. Acta 1708, 23–34 (2005)
(
10.1016/j.bbabio.2004.12.010
) / Biochim. Biophys. Acta by R van Lis (2005) -
Atteia, A., van Lis, R., Ramírez, J. & González-Halphen, D. Polytomella spp. growth on ethanol: extracellular pH affects the accumulation of mitochondrial cytochrome c550 . Eur. J. Biochem. 267, 2850–2858 (2000)
(
10.1046/j.1432-1327.2000.01288.x
) / Eur. J. Biochem. by A Atteia (2000) -
Vázquez-Acevedo, M. et al. The mitochondrial ATP synthase of chlorophycean algae contains eight subunits of unknown origin involved in the formation of an atypical stator-stalk and in the dimerization of the complex. J. Bioenerg. Biomembr. 38, 271–282 (2006)
(
10.1007/s10863-006-9046-x
) / J. Bioenerg. Biomembr. by M Vázquez-Acevedo (2006) -
Villavicencio-Queijeiro, A. et al. The fully-active and structurally-stable form of the mitochondrial ATP synthase of Polytomella sp. is dimeric. J. Bioenerg. Biomembr. 41, 1–13 (2009)
(
10.1007/s10863-009-9203-0
) / J. Bioenerg. Biomembr. by A Villavicencio-Queijeiro (2009) -
Mills, D. J., Vitt, S., Strauss, M., Shima, S. & Vonck, J. De novo modeling of the F420-reducing [NiFe]-hydrogenase from a methanogenic archaeon by cryo-electron microscopy. eLife 2, e00218 (2013)
(
10.7554/eLife.00218
) / eLife by DJ Mills (2013) -
Allegretti, M., Mills, D. J., McMullan, G., Kühlbrandt, W. & Vonck, J. Atomic model of the F420-reducing [NiFe] hydrogenase by electron cryo-microscopy using a direct electron detector. eLife 3, e01963 (2014)
(
10.7554/eLife.01963
) / eLife by M Allegretti (2014) -
Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nature Methods 10, 584–590 (2013)
(
10.1038/nmeth.2472
) / Nature Methods by X Li (2013) -
Mindell, J. A. & Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334–347 (2003)
(
10.1016/S1047-8477(03)00069-8
) / J. Struct. Biol. by JA Mindell (2003) -
Scheres, S. H. W. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519–530 (2012)
(
10.1016/j.jsb.2012.09.006
) / J. Struct. Biol. by SHW Scheres (2012) -
Wong, W. et al. Cryo-EM structure of the Plasmodium falciparum 80S ribosome bound to the anti-protozoan drug emetine. eLife 3, e3080 (2014)
(
10.7554/eLife.03080
) / eLife by W Wong (2014) -
Ludtke, S. J., Baldwin, P. R. & Chiu, W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128, 82–97 (1999)
(
10.1006/jsbi.1999.4174
) / J. Struct. Biol. by SJ Ludtke (1999) -
Davies, K. M., Anselmi, C., Wittig, I., Faraldo-Gomez, J. D. & Kuhlbrandt, W. Structure of the yeast F1Fo-ATP synthase dimer and its role in shaping the mitochondrial cristae. Proc. Natl Acad. Sci. USA 109, 13602–13607 (2012)
(
10.1073/pnas.1204593109
) / Proc. Natl Acad. Sci. USA by KM Davies (2012) -
Scheres, S. H. W. Beam-induced motion correction for sub-megadalton cryo-EM particles. eLife 3, e03665 (2014)
(
10.7554/eLife.03665
) / eLife by SHW Scheres (2014) -
Chen, S. et al. High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 135, 24–35 (2013)
(
10.1016/j.ultramic.2013.06.004
) / Ultramicroscopy by S Chen (2013) -
Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nature Methods 11, 63–65 (2014)
(
10.1038/nmeth.2727
) / Nature Methods by A Kucukelbir (2014) -
Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38–46 (2007)
(
10.1016/j.jsb.2006.05.009
) / J. Struct. Biol. by G Tang (2007) -
Larkin, M. A. et al. Clustal W and Clustal X version 2.0. Bioinformatics 23, 2947–2948 (2007)
(
10.1093/bioinformatics/btm404
) / Bioinformatics by MA Larkin (2007) -
Schroeder, G. F., Brunger, A. T. & Levitt, M. Combining efficient conformational sampling with a deformable elastic network model facilitates structure refinement at low resolution. Structure 15, 1630–1641 (2007)
(
10.1016/j.str.2007.09.021
) / Structure by GF Schroeder (2007) -
Pettersen, E. F. et al. UCSF Chimera: a visualisation system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004)
(
10.1002/jcc.20084
) / J. Comput. Chem. by EF Pettersen (2004) -
Wada, T., Long, J. C., Zhang, D. & Vik, S. B. A novel labeling approach supports the five-transmembrane model of subunit a of the Escherichia coli ATP synthase. J. Biol. Chem. 274, 17353–17357 (1999)
(
10.1074/jbc.274.24.17353
) / J. Biol. Chem. by T Wada (1999) -
Careaga, C. L. & Falke, J. J. Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor: detection by disulfide trapping. J. Mol. Biol. 226, 1219–1235 (1992)
(
10.1016/0022-2836(92)91063-U
) / J. Mol. Biol. by CL Careaga (1992) -
Vincent, O. D., Schwem, B. E., Steed, P. R., Jiang, W. & Fillingame, R. H. Fluidity of structure and swiveling of helices in the subunit c ring of Escherichia coli ATP synthase as revealed by cysteine-cysteine cross-linking. J. Biol. Chem. 282, 33788–33794 (2007).
(
10.1074/jbc.M706904200
) / J. Biol. Chem. by OD Vincent (2007)
Dates
Type | When |
---|---|
Created | 10 years, 5 months ago (Feb. 24, 2015, 7:12 a.m.) |
Deposited | 2 years, 3 months ago (May 18, 2023, 2:28 p.m.) |
Indexed | 2 days, 20 hours ago (Aug. 19, 2025, 5:58 a.m.) |
Issued | 10 years, 5 months ago (Feb. 23, 2015) |
Published | 10 years, 5 months ago (Feb. 23, 2015) |
Published Online | 10 years, 5 months ago (Feb. 23, 2015) |
Published Print | 10 years, 3 months ago (May 1, 2015) |
@article{Allegretti_2015, title={Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase}, volume={521}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/nature14185}, DOI={10.1038/nature14185}, number={7551}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Allegretti, Matteo and Klusch, Niklas and Mills, Deryck J. and Vonck, Janet and Kühlbrandt, Werner and Davies, Karen M.}, year={2015}, month=feb, pages={237–240} }