Publications
71 results found
Pogoryelov D, Meier T, 2008, What determines the size of the F<sub>o</sub> rotor?, 15th European Bioenergetics Conference, Publisher: ELSEVIER SCIENCE BV, Pages: S17-S17, ISSN: 0005-2728
Pogoryelov D, Schlattner U, Meier T, et al., 2008, The rotor subunit interface of the ATP synthase from <i>Ilyobacter tartaricus</i>, BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Vol: 1777, Pages: S17-S17, ISSN: 0005-2728
Fritz M, Klyszejko AL, Morgner N, et al., 2008, An intermediate step in the evolution of ATPases -: a hybrid F<sub>0</sub>-V<sub>0</sub> rotor in a bacterial Na<SUP>+</SUP>F<sub>1</sub>F<sub>0</sub> ATP synthase, FEBS JOURNAL, Vol: 275, Pages: 1999-2007, ISSN: 1742-464X
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- Citations: 46
Meier T, Morgner N, Matthies D, et al., 2007, A tridecameric c ring of the adenosine triphosphate (ATP) synthase from the thermoalkaliphilic <i>Bacillus</i> sp strain TA2.A1 facilitates ATP synthesis at low electrochemical proton potential, MOLECULAR MICROBIOLOGY, Vol: 65, Pages: 1181-1192, ISSN: 0950-382X
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- Citations: 76
Pogoryelov D, Reichen C, Klyszejko AL, et al., 2007, The oligomeric state of c rings from cyanobacterial F-ATP synthases varies from 13 to 15, JOURNAL OF BACTERIOLOGY, Vol: 189, Pages: 5895-5902, ISSN: 0021-9193
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- Citations: 79
Meier T, Ferguson SA, Cook GM, et al., 2006, Structural investigations of the membrane-embedded rotor ring of the F-ATPase from <i>Clostridium paradoxum</i>, JOURNAL OF BACTERIOLOGY, Vol: 188, Pages: 7759-7764, ISSN: 0021-9193
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- Citations: 51
Meier T, Polzer P, Diederichs K, et al., 2005, Structure of the Rotor Ring of F-Type Na <sup>+</sup> -ATPase from <i>Ilyobacter tartaricus</i>, Science, Vol: 308, Pages: 659-662, ISSN: 0036-8075
<jats:p> In the crystal structure of the membrane-embedded rotor ring of the sodium ion–translocating adenosine 5′-triphosphate (ATP) synthase of <jats:italic>Ilyobacter tartaricus</jats:italic> at 2.4 angstrom resolution, 11 c subunits are assembled into an hourglass-shaped cylinder with 11-fold symmetry. Sodium ions are bound in a locked conformation close to the outer surface of the cylinder near the middle of the membrane. The structure supports an ion-translocation mechanism in the intact ATP synthase in which the binding site converts from the locked conformation into one that opens toward subunit a as the rotor ring moves through the subunit a/c interface. </jats:p>
Meier T, Matthey U, von Ballmoos C, et al., 2003, Evidence for structural integrity in the undecameric c-rings isolated from sodium ATP synthases, JOURNAL OF MOLECULAR BIOLOGY, Vol: 325, Pages: 389-397, ISSN: 0022-2836
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- Citations: 73
Vonck J, von Nidda TK, Meier T, et al., 2002, Molecular architecture of the undecameric rotor of a bacterial Na<SUP>+</SUP>-ATP synthase, JOURNAL OF MOLECULAR BIOLOGY, Vol: 321, Pages: 307-316, ISSN: 0022-2836
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- Citations: 96
Meier T, Matthey U, Henzen F, et al., 2001, The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids, FEBS Letters, Vol: 505, Pages: 353-356, ISSN: 0014-5793
<jats:p>The isolated rotor cylinder of the ATP synthase from <jats:italic>Ilyobacter tartaricus</jats:italic> was reconstituted into two‐dimensional crystalline arrays. Atomic force microscopy imaging indicated a central cavity on one side of the rotor and a central plug protruding from the other side. Upon incubation with phospholipase C, the plug disappeared, but the appearance of the surrounding c subunit oligomer was not affected. This indicates that the plug consists of phospholipids. As the detergent‐purified c cylinder is completely devoid of phospholipids, these are incorporated into the central hole from one side of the cylinder during the reconstitution procedure.</jats:p>
Müller DJ, Dencher NA, Meier T, et al., 2001, ATP synthase: constrained stoichiometry of the transmembrane rotor, FEBS Letters, Vol: 504, Pages: 219-222, ISSN: 0014-5793
<jats:p>Recent structural data suggest that the number of identical subunits (<jats:italic>c</jats:italic> or III) assembled into the cation‐powered rotor of F<jats:sub>1</jats:sub>F<jats:sub>0</jats:sub> ATP synthase depends on the biological origin. Atomic force microscopy allowed individual subunits of the cylindrical transmembrane rotors from spinach chloroplast and from <jats:italic>Ilyobacter tartaricus</jats:italic> ATP synthase to be directly visualized in their native‐like environment. Occasionally, individual rotors exhibit structural gaps of the size of one or more subunits. Complete rotors and arch‐shaped fragments of incomplete rotors revealed the same diameter within one ATP synthase species. These results suggest the rotor diameter and stoichiometry to be determined by the shape of the subunits and their nearest neighbor interactions.</jats:p>
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