scholarly journals The crystallographic structure of subunit E from Pyrococcus horikoshii OT3 A-ATP synthase reveals the flexibility of the peripheral stalk

2012 ◽  
Vol 1817 ◽  
pp. S10-S11
Author(s):  
A.M. Balakrishna ◽  
G. Grüber
Keyword(s):  
Atp Synthase ◽  
Crystallographic Structure ◽  
Pyrococcus Horikoshii ◽  
Peripheral Stalk ◽  
Subunit E

scholarly journals Crystallographic structure of the turbine C-ring from spinach chloroplast F-ATP synthase

2014 ◽  
Vol 34 (2) ◽  
Author(s):  
Asha Manikkoth Balakrishna ◽  
Holger Seelert ◽  
Sven-Hendric Marx ◽  
Norbert A. Dencher ◽  
Gerhard Grüber
Keyword(s):  
Atp Synthase ◽  
Ring Width ◽  
Atp Synthesis ◽  
Crystallographic Structure ◽  
Unit Cell Parameters ◽  
Subunit C ◽  
Cell Parameters ◽  
Ring Diameter ◽  
C Subunit

In eukaryotic and prokaryotic cells, F-ATP synthases provide energy through the synthesis of ATP. The chloroplast F-ATP synthase (CF1FO-ATP synthase) of plants is integrated into the thylakoid membrane via its FO-domain subunits a, b, b’ and c. Subunit c with a stoichiometry of 14 and subunit a form the gate for H+-pumping, enabling the coupling of electrochemical energy with ATP synthesis in the F1 sector. Here we report the crystallization and structure determination of the c14-ring of subunit c of the CF1FO-ATP synthase from spinach chloroplasts. The crystals belonged to space group C2, with unit-cell parameters a=144.420, b=99.295, c=123.51 Å, and β=104.34° and diffracted to 4.5 Å resolution. Each c-ring contains 14 monomers in the asymmetric unit. The length of the c-ring is 60.32 Å, with an outer ring diameter 52.30 Å and an inner ring width of 40 Å.

scholarly journals The INA complex facilitates assembly of the peripheral stalk of the mitochondrial F 1 F o ‐ ATP synthase

2014 ◽  
Vol 33 (15) ◽  
pp. 1624-1638 ◽  
Author(s):  
Oleksandr Lytovchenko ◽  
Nataliia Naumenko ◽  
Silke Oeljeklaus ◽  
Bernhard Schmidt ◽  
Karina Malsburg ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Peripheral Stalk

Complete amino acid sequence of subunit e of rat liver mitochondrial hydrogen ion-ATP synthase

Biochemistry ◽  
1992 ◽  
Vol 31 (49) ◽  
pp. 12451-12454 ◽  
Author(s):  
Tomihiko Higuti ◽  
Kayo Kuroiwa ◽  
Yoshihiro Kawamura ◽  
Yutaka Yoshihara
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Atp Synthase ◽  
Rat Liver ◽  
Hydrogen Ion ◽  
Complete Amino Acid Sequence ◽  
Subunit E

Biophysics and Bioinformatics Reveal Structural Differences of the Two Peripheral Stalk Subunits in Chloroplast ATP Synthase

2006 ◽  
Vol 141 (3) ◽  
pp. 411-420 ◽  
Author(s):  
A. Poetsch ◽  
R. J. Berzborn ◽  
J. Heberle ◽  
T. A. Link ◽  
N. A. Dencher ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Peripheral Stalk ◽  
Chloroplast Atp Synthase ◽  
Structural Differences

scholarly journals The Proton-translocatingaSubunit of F0F1-ATP Synthase Is Allocated Asymmetrically to the Peripheral Stalk

2008 ◽  
Vol 283 (48) ◽  
pp. 33602-33610 ◽  
Author(s):  
Monika G. Düser ◽  
Yumin Bi ◽  
Nawid Zarrabi ◽  
Stanley D. Dunn ◽  
Michael Börsch
Keyword(s):  
Atp Synthase ◽  
Peripheral Stalk ◽  
F0f1 Atp Synthase

scholarly journals Intergenic suppression of the γM23K uncoupling mutation in F0F1 ATP synthase by βGlu-381 substitutions: the role of the β380DELSEED386 segment in energy coupling

1998 ◽  
Vol 330 (2) ◽  
pp. 707-712 ◽  
Author(s):  
J. Christian KETCHUM ◽  
Marwan K. AL-SHAWI ◽  
K. Robert NAKAMOTO
Keyword(s):  
Hydrogen Bond ◽  
Transition State ◽  
Thermodynamic Parameters ◽  
Atp Synthase ◽  
Energy Coupling ◽  
Crystallographic Structure ◽  
Β Subunit ◽  
Wild Type ◽  
F0f1 Atp Synthase

We previously demonstrated that the Escherichia coli F0F1-ATP synthase mutation, γM23K, caused increased energy of interaction between γ- and β-subunits which was correlated to inefficient coupling between catalysis and transport [Al-Shawi, Ketchum and Nakamoto (1997) J. Biol. Chem. 272, 2300-2306]. Based on these results and the X-ray crystallographic structure of bovine F1-ATPase [Abrahams, Leslie, Lutter and Walker (1994) Nature (London) 370, 621-628] γM23K is believed to form an ionized hydrogen bond with βGlu-381 in the conserved β380DELSEED386 segment. In this report, we further test the role of γ-β-subunit interactions by introducing a series of substitutions for βGlu-381 and γArg-242, the residue which forms a hydrogen bond with βGlu-381 in the wild-type enzyme. βE381A, D, and Q were able to restore efficient coupling when co-expressed with γM23K. All three mutations reversed the increased transition state thermodynamic parameters for steady state ATP hydrolysis caused by γM23K. βE381K by itself caused inefficient coupling, but opposite from the effect of γM23K, the transition state thermodynamic parameters were lower than wild-type. These results suggest that the βE381K mutation perturbs the γ-β-subunit interaction and the local conformation of the β380DELSEED386 segment in a specific way that disrupts the communication of coupling information between transport and catalysis. βE381A, L, K, and R, and γR242L and E mutations perturbed enzyme assembly and stability to varying degrees. These results provide functional evidence that the β380DELSEED386 segment and its interactions with the γ-subunit are involved in the mechanism of coupling.

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