The Structural and Functional Role of the y-e Rotor in Escherichia Coli F0F1 ATP Synthase

2008 ◽  
Author(s):  
Shin-Kai Lin
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Functional Role ◽  
F0f1 Atp Synthase

Turnover Number of Escherichia coli F0F1 ATP Synthase for ATP Synthesis in Membrane Vesicles

1997 ◽  
Vol 243 (1-2) ◽  
pp. 336-343 ◽  
Author(s):  
Carsten Etzold ◽  
Gabriele Deckers-Hebestreit ◽  
Karlheinz Altendorf
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Atp Synthesis ◽  
Membrane Vesicles ◽  
Turnover Number ◽  
F0f1 Atp Synthase

scholarly journals An alternative role of FoF1-ATP synthase in Escherichia coli: synthesis of thiamine triphosphate

2013 ◽  
Vol 3 (1) ◽  
Author(s):  
Tiziana Gigliobianco ◽  
Marjorie Gangolf ◽  
Bernard Lakaye ◽  
Bastien Pirson ◽  
Christoph von Ballmoos ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Thiamine Triphosphate ◽  
Fof1 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.

Investigation of the functional role of tryptophan-22 in Escherichia coli dihydrofolate reductase by site-directed mutagenesis

Biochemistry ◽  
1991 ◽  
Vol 30 (46) ◽  
pp. 11092-11103 ◽  
Author(s):  
Mark S. Warren ◽  
Katherine A. Brown ◽  
Martin F. Farnum ◽  
Elizabeth E. Howell ◽  
Joseph Kraut
Keyword(s):  
Escherichia Coli ◽  
Dihydrofolate Reductase ◽  
Functional Role ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

scholarly journals Analysis of the functional role of conserved residues in the protein subunit of ribonuclease P from Escherichia coli

1997 ◽  
Vol 267 (4) ◽  
pp. 818-829 ◽  
Author(s):  
Venkat Gopalan ◽  
Andreas D Baxevanis ◽  
David Landsman ◽  
Sidney Altman
Keyword(s):  
Escherichia Coli ◽  
Functional Role ◽  
Ribonuclease P ◽  
Protein Subunit ◽  
Conserved Residues
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