Publications
71 results found
Matthies D, Klyszejko AL, Brandt K, et al., 2012, Structure of the F<sub>o</sub>/V<sub>o</sub>-hybrid ATP synthase rotor ring from <i>Acetobacterium woodii</i> at 2.4 Å resolution, Publisher: ELSEVIER SCIENCE BV, Pages: S19-S19, ISSN: 0005-2728
Pogoryelov D, Klyszejko AL, Krasnoselska GO, et al., 2012, Engineering rotor ring stoichiometries in the ATP synthase, BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Vol: 1817, Pages: S21-S21, ISSN: 0005-2728
Schulz S, Krah A, Yildiz O, et al., 2012, High-resolution structure of a Na<SUP>+</SUP>-driven ATP synthase rotor ring with a two-carboxylate ion-binding motif, Publisher: ELSEVIER SCIENCE BV, Pages: S23-S23, ISSN: 0005-2728
Denys P, Krasnoselska G, Klyszejko A, et al., 2012, Bioengineering of the ATP synthase: customized ion-to-ATP ratios and ion specificity, 22nd IUBMB Congress/37th FEBS Congress, Publisher: WILEY-BLACKWELL, Pages: 120-120, ISSN: 1742-464X
Hakulinen JK, Klyszejko AL, Hoffmann J, et al., 2012, Structural study on the architecture of the bacterial ATP synthase F<sub>o</sub> motor, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 109, Pages: E2050-E2056, ISSN: 0027-8424
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- Citations: 26
Pogoryelov D, Klyszejko AL, Krasnoselska GO, et al., 2012, Engineering rotor ring stoichiometries in the ATP synthase, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 109, Pages: E1599-E1608, ISSN: 0027-8424
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- Citations: 71
Symersky J, Pagadala V, Osowski D, et al., 2012, Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation, Nature Structural and Molecular Biology, Vol: 19, Pages: 485-491, ISSN: 1545-9985
The proton pore of the F1Fo ATP synthase consists of a ring of c subunits, which rotates, driven by downhill proton diffusion across the membrane. An essential carboxylate side chain in each subunit provides a proton-binding site. In all the structures of c-rings reported to date, these sites are in a closed, ion-locked state. Structures are here presented of the c10 ring from Saccharomyces cerevisiae determined at pH 8.3, 6.1 and 5.5, at resolutions of 2.0 Å, 2.5 Å and 2.0 Å, respectively. The overall structure of this mitochondrial c-ring is similar to known homologs, except that the essential carboxylate, Glu59, adopts an open extended conformation. Molecular dynamics simulations reveal that opening of the essential carboxylate is a consequence of the amphiphilic nature of the crystallization buffer. We propose that this new structure represents the functionally open form of the c subunit, which facilitates proton loading and release.
Hammann E, Zappe A, Keis S, et al., 2012, Step size of the rotary proton motor in single F<sub>o</sub>F<sub>1</sub>-ATP synthase from a thermoalkaliphilic bacterium by DCO-ALEX FRET, Conference on Single Molecule Spectroscopy and Super-Resolution Imaging V, Publisher: SPIE-INT SOC OPTICAL ENGINEERING, ISSN: 0277-786X
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- Citations: 7
McMillan DGG, Ferguson SA, Dey D, et al., 2011, A<sub>1</sub>A<sub>o</sub>-ATP Synthase of <i>Methanobrevibacter ruminantium</i> Couples Sodium Ions for ATP Synthesis under Physiological Conditions, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 286, Pages: 39882-39892
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- Citations: 32
Matthies D, Haberstock S, Joos F, et al., 2011, Cell-Free Expression and Assembly of ATP Synthase, JOURNAL OF MOLECULAR BIOLOGY, Vol: 413, Pages: 593-603, ISSN: 0022-2836
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- Citations: 70
Kalamorz F, Keis S, McMillan DGG, et al., 2011, Draft Genome Sequence of the Thermoalkaliphilic <i>Caldalkalibacillus thermarum</i> Strain TA2.A1, JOURNAL OF BACTERIOLOGY, Vol: 193, Pages: 4290-4291, ISSN: 0021-9193
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- Citations: 11
Liu J, Fackelmayer OJ, Hicks DB, et al., 2011, Mutations in a Helix-1 Motif of the ATP Synthase c-Subunit of <i>Bacillus pseudofirmus</i> OF4 Cause Functional Deficits and Changes in the <i>c</i>-Ring Stability and Mobility on Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis, BIOCHEMISTRY, Vol: 50, Pages: 5497-5506, ISSN: 0006-2960
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- Citations: 8
Pogoryelov D, Krah A, Langer JD, et al., 2010, Microscopic rotary mechanism of ion translocation in the F<sub>0</sub> complex of ATP synthases, NATURE CHEMICAL BIOLOGY, Vol: 6, Pages: 891-899, ISSN: 1552-4450
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- Citations: 114
Preiss L, Yildiz O, Hicks DB, et al., 2010, A new type of proton coordination in an F1Fo-ATP synthase rotor ring, PLoS Biology, Vol: 8, Pages: 1-10, ISSN: 1544-9173
We solved the crystal structure of a novel type of c-ring isolated from Bacillus pseudofirmus OF4 at 2.5 Å, revealing a cylinder with a tridecameric stoichiometry, a central pore, and an overall shape that is distinct from those reported thus far. Within the groove of two neighboring c-subunits, the conserved glutamate of the outer helix shares the proton with a bound water molecule which itself is coordinated by three other amino acids of outer helices. Although none of the inner helices contributes to ion binding and the glutamate has no other hydrogen bonding partner than the water oxygen, the site remains in a stable, ion-locked conformation that represents the functional state present at the c-ring/membrane interface during rotation. This structure reveals a new, third type of ion coordination in ATP synthases. It appears in the ion binding site of an alkaliphile in which it represents a finely tuned adaptation of the proton affinity during the reaction cycle.
Liu J, Fackelmayer O, Preiss L, et al., 2010, Single, double and triple alanine to glycine replacements in the AxAxAxA motif of alkaliphilic <i>Bacillus pseudofirmus</i> OF4 c-subunits affect c-ring stability, change both monomer and c-ring mobility in SDS-PAGE and lead to deficits in ATP synthesis, 16th European Bioenergetics Conference, Publisher: ELSEVIER SCIENCE BV, Pages: 35-36, ISSN: 0005-2728
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- Citations: 5
Meier T, 2010, Structural basis of ion binding modes in the F<sub>o</sub> rotor of H<SUP>+</SUP> and Na <SUP>+</SUP> translocating ATP synthases, 16th European Bioenergetics Conference, Publisher: ELSEVIER SCIENCE BV, Pages: 26-26, ISSN: 0005-2728
Pogoryelov D, Krah A, Langer J, et al., 2010, On the rotary mechanism of F<sub>1</sub>F<sub>o</sub>-ATP synthases, 16th European Bioenergetics Conference, Publisher: ELSEVIER SCIENCE BV, Pages: 37-37, ISSN: 0005-2728
Krah A, Pogoryelov D, Langer J, et al., 2010, Structural basis for the ion selectivity of F-ATP-synthase c-ring rotors, BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Vol: 1797, Pages: 35-35, ISSN: 0005-2728
Hakulinen J, Hoffmann J, Eckhardt-Strelau L, et al., 2010, Biochemical and structural investigations of the <i>Hyobacter tartaricus</i> F<sub>0</sub> ATP synthase, 16th European Bioenergetics Conference, Publisher: ELSEVIER SCIENCE BV, Pages: 33-33, ISSN: 0005-2728
Matthies D, Preiss L, Morgner N, et al., 2010, Structural studies of the membrane-embedded c-ring of the FIFO-ATP synthase from a thermoalkaliphilic bacterium reveal a strategy for adaptation to alkaline environments, 16th European Bioenergetics Conference, Publisher: ELSEVIER SCIENCE BV, Pages: 36-36, ISSN: 0005-2728
Pogoryelov D, Krah A, Langer J, et al., 2010, On the rotary mechanism and ion binding specificity of F1Fo-ATP synthases, 35th Congress of the Federation-of-European-Biochemical-Societies, Publisher: WILEY-BLACKWELL PUBLISHING, INC, Pages: 213-213, ISSN: 1742-464X
Krah A, Pogoryelov D, Langer JD, et al., 2010, Structural and energetic basis for H<SUP>+</SUP> versus Na<SUP>+</SUP> binding selectivity in ATP synthase F<sub>o</sub> rotors, 16th European Bioenergetics Conference, Publisher: ELSEVIER, Pages: 763-772, ISSN: 0005-2728
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- Citations: 52
Krah A, Pogoryelov D, Meier T, et al., 2010, On the Structure of the Proton-Binding Site in the F<sub>o</sub> Rotor of Chloroplast ATP Synthases, JOURNAL OF MOLECULAR BIOLOGY, Vol: 395, Pages: 20-27, ISSN: 0022-2836
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- Citations: 34
Hoffmann J, Sokolova L, Preiss L, et al., 2010, ATP synthases: cellular nanomotors characterized by LILBID mass spectrometry, PHYSICAL CHEMISTRY CHEMICAL PHYSICS, Vol: 12, Pages: 13375-13382, ISSN: 1463-9076
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- Citations: 15
Pogoryelov D, Yildiz O, Faraldo-Gomez JD, et al., 2009, High-resolution structure of the rotor ring of a proton-dependent ATP synthase, NATURE STRUCTURAL & MOLECULAR BIOLOGY, Vol: 16, Pages: 1068-U88, ISSN: 1545-9993
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- Citations: 152
Meier T, Krah A, Bond PJ, et al., 2009, Complete Ion-Coordination Structure in the Rotor Ring of Na<SUP>+</SUP>-Dependent F-ATP Synthases, JOURNAL OF MOLECULAR BIOLOGY, Vol: 391, Pages: 498-507, ISSN: 0022-2836
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- Citations: 81
Matthies D, Preiss L, Klyszejko AL, et al., 2009, The c<sub>13</sub> Ring from a Thermoalkaliphilic ATP Synthase Reveals an Extended Diameter Due to a Special Structural Region, JOURNAL OF MOLECULAR BIOLOGY, Vol: 388, Pages: 611-618, ISSN: 0022-2836
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- Citations: 54
Morgner N, Hoffmann J, Barth H-D, et al., 2008, LILBID-mass spectrometry applied to the mass analysis of RNA polymerase II and an F<sub>1</sub>F<sub>o</sub>-ATP synthase, INTERNATIONAL JOURNAL OF MASS SPECTROMETRY, Vol: 277, Pages: 309-313, ISSN: 1387-3806
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- Citations: 17
Pogoryelov D, Nikolaev Y, Schlattner U, et al., 2008, Probing the rotor subunit interface of the ATP synthase from <i>Ilyobacter tartaricus</i>, FEBS JOURNAL, Vol: 275, Pages: 4850-4862, ISSN: 1742-464X
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- Citations: 27
Meier T, Morgner N, Matthies D, et al., 2008, Mass determination of membrane protein complexes in detergent solution: The c rings from F-ATP synthases, 15th European Bioenergetics Conference, Publisher: ELSEVIER SCIENCE BV, Pages: S19-S20, ISSN: 0005-2728
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