Low resolution structure of subunit b (b 22–156) of Escherichia coli F1FO ATP synthase in solution and the b−δ assembly

2008 ◽  
Vol 40 (4) ◽  
pp. 245-255 ◽  
Author(s):  
Ragunathan Priya ◽  
Vikeramjeet S. Tadwal ◽  
Manfred W. Roessle ◽  
Shovanlal Gayen ◽  
Cornelia Hunke ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Low Resolution ◽  
F1fo Atp Synthase ◽  
Subunit B ◽  
Resolution Structure

The transmembrane domain of subunit b of the Escherichia coli F1FO ATP synthase is sufficient for H+-translocating activity together with subunits a and c

2004 ◽  
Vol 271 (14) ◽  
pp. 3036-3042 ◽  
Author(s):  
Jörg-Christian Greie ◽  
Thomas Heitkamp ◽  
Karlheinz Altendorf
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Transmembrane Domain ◽  
F1fo Atp Synthase ◽  
Subunit B

Subunit II (b') and Not Subunit I (b) of Photosynthetic ATP Synthases is Equivalent to Subunit b of the ATP Synthases from Nonphotosynthetic Eubacteria. Evidence for a New Assignment of b-Type F0 Subunits

1997 ◽  
Vol 52 (11-12) ◽  
pp. 789-798 ◽  
Author(s):  
Hans-Jürgen Tiburzy ◽  
Richard J. Berzborn
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Structural Feature ◽  
Atp Synthase ◽  
Primary Structure ◽  
Structural Features ◽  
Amino Acid Sequences ◽  
E Coli ◽  
Subunit B ◽  
Atp Synthases

Abstract Subunit I of chloroplast ATP synthase is reviewed until now to be equivalent to subunit b of Escherichia coli ATP synthase, whereas subunit II is suggested to be an additional subunit in photosynthetic ATP synthases lacking a counterpart in E. coli. After publication of some sequences of subunits II a revision of this assignment is necessary. Based on the analysis of 51 amino acid sequences of b-type subunits concerning similarities in primary structure, iso­electric point and a discovered discontinuous structural feature, our data provide evidence that chloroplast subunit II (subunit b' of photosynthetic eubacteria) and not chloroplast subunit I (subunit b of photosynthetic eubacteria) is the equivalent of subunit b of nonphoto­ synthetic eubacteria, and therefore does have a counterpart in e.g. E. coli. In consequence, structural features essential for function should be looked for on subunit II (b').

scholarly journals S1.32 Intermediate positions of ATP on its trail to the binding pocket of subunit B and the high resolution structure of its neighbouring subunit F of the A1AO A1A0 ATP synthase

2008 ◽  
Vol 1777 ◽  
pp. S17
Author(s):  
Anil Kumar ◽  
Malathy S.S. Manimekalai ◽  
Asha M. Balakrishna ◽  
Shovanlal Gayen ◽  
Subramanian Vivekanandan ◽  
...  
Keyword(s):  
High Resolution ◽  
Atp Synthase ◽  
Binding Pocket ◽  
High Resolution Structure ◽  
Subunit B ◽  
Resolution Structure

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

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 Substitution of the cysteinyl residue (Cys21) of subunit b of the ATP synthase from Escherichia coli

1991 ◽  
Vol 202 (3) ◽  
pp. 1307-1312 ◽  
Author(s):  
Sabine KAUFFER ◽  
Gabriele DECKERS-HEBESTREIT ◽  
Karlheinz ALTENDORF
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Subunit B ◽  
Cysteinyl Residue

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
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