scholarly journals Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking

1998 ◽  
Vol 95 (12) ◽  
pp. 6607-6612 ◽  
Author(s):  
W. Jiang ◽  
R. H. Fillingame
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Cross Linking ◽  
F1fo Atp Synthase

scholarly journals A functionally inactive, cold-stabilized form of the Escherichia coli F1Fo ATP synthase

2006 ◽  
Vol 1757 (3) ◽  
pp. 206-214 ◽  
Author(s):  
Mikhail A. Galkin ◽  
Robert R. Ishmukhametov ◽  
Steven B. Vik
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
F1fo Atp Synthase

Production of fully assembled and active Aquifex aeolicus F1FO ATP synthase in Escherichia coli

2014 ◽  
Vol 1840 (1) ◽  
pp. 34-40 ◽  
Author(s):  
Chunli Zhang ◽  
Matteo Allegretti ◽  
Janet Vonck ◽  
Julian D. Langer ◽  
Marco Marcia ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Aquifex Aeolicus ◽  
F1fo Atp Synthase

Cross-linking and electron microscopy studies of the structure and functioning of the Escherichia coli ATP synthase

2000 ◽  
Vol 203 (1) ◽  
pp. 29-33 ◽  
Author(s):  
R.A. Capaldi ◽  
B. Schulenberg ◽  
J. Murray ◽  
R. Aggeler
Keyword(s):  
Electron Microscopy ◽  
Escherichia Coli ◽  
Oxidative Phosphorylation ◽  
Atp Synthase ◽  
Proton Gradient ◽  
Cross Linking ◽  
Combination Of Methods ◽  
Chemical Cross Linking

ATP synthase, also called F(1)F(o)-ATPase, catalyzes the synthesis of ATP during oxidative phosphorylation. The enzyme is reversible and is able to use ATP to drive a proton gradient for transport purposes. Our work has focused on the enzyme from Escherichia coli (ECF(1)F(o)). We have used a combination of methods to study this enzyme, including electron microscopy and chemical cross-linking. The utility of these two approaches in particular, and the important insights they give into the structure and mechanism of the ATP synthase, are reviewed.

Functional production of the Na+ F1FO ATP synthase from Acetobacterium woodii in Escherichia coli requires the native AtpI

2012 ◽  
Vol 45 (1-2) ◽  
pp. 15-23 ◽  
Author(s):  
Karsten Brandt ◽  
Daniel B. Müller ◽  
Jan Hoffmann ◽  
Christine Hübert ◽  
Bernd Brutschy ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Acetobacterium Woodii ◽  
F1fo Atp Synthase

scholarly journals Expression, purification and crystallization of central stalk and peripheral stalk of F1Fo ATP synthase from Aquifex aeolicus in Escherichia coli

2012 ◽  
Vol 1817 ◽  
pp. S27
Author(s):  
Shuai Xin ◽  
Chunli Zhang ◽  
Julian Langer ◽  
Guohong Peng ◽  
Hartmut Michel
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Aquifex Aeolicus ◽  
F1fo Atp Synthase ◽  
Peripheral Stalk ◽  
Central Stalk

scholarly journals Fluidity of Structure and Swiveling of Helices in the Subunit c Ring of Escherichia coli ATP Synthase as Revealed by Cysteine-Cysteine Cross-Linking

2007 ◽  
Vol 282 (46) ◽  
pp. 33788-33794 ◽  
Author(s):  
Owen D. Vincent ◽  
Brian E. Schwem ◽  
P. Ryan Steed ◽  
Warren Jiang ◽  
Robert H. Fillingame
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Time Course ◽  
Structural Model ◽  
Ring Structure ◽  
High Yield ◽  
Cross Linking ◽  
E Coli ◽  
The Cross ◽  
Ilyobacter Tartaricus

Subunit c in the membrane-traversing F0 sector of Escherichia coli ATP synthase is known to fold with two transmembrane helices and form an oligomeric ring of 10 or more subunits in the membrane. Models for the E. coli ring structure have been proposed based upon NMR solution structures and intersubunit cross-linking of Cys residues in the membrane. The E. coli models differ from the recent x-ray diffraction structure of the isolated Ilyobacter tartaricus c-ring. Furthermore, key cross-linking results supporting the E. coli model prove to be incompatible with the I. tartaricus structure. To test the applicability of the I. tartaricus model to the E. coli c-ring, we compared the cross-linking of a pair of doubly Cys substituted c-subunits, each of which was compatible with one model but not the other. The key finding of this study is that both A21C/M65C and A21C/I66C doubly substituted c-subunits form high yield oligomeric structures, c2, c3... c10, via intersubunit disulfide bond formation. The results indicate that helical swiveling, with resultant interconversion of the two conformers predicted by the E. coli and I. tartaricus models, must be occurring over the time course of the cross-linking experiment. In the additional experiments reported here, we tried to ascertain the preferred conformation in the membrane to help define the most likely structural model. We conclude that both structures must be able to form in the membrane, but that the helical swiveling that promotes their interconversion may not be necessary during rotary function.

The b arg36 contributes to efficient coupling in F1FO ATP synthase in Escherichia coli

2008 ◽  
Vol 40 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Amanda K. Welch ◽  
Shane B. Claggett ◽  
Brian D. Cain
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
F1fo Atp Synthase ◽  
Efficient Coupling
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