Conformational changes in the Escherichia coli ATP synthase b-dimer upon binding to F1-ATPase
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Physiology
Link
http://link.springer.com/content/pdf/10.1007/s10863-008-9189-z.pdf
Reference36 articles.
1. Bhatt D, Cole SP, Grabar TB, Claggett SB, Cain BD (2005) Manipulating the length of the b ubunit F1 binding domain in F1F0 ATP synthase from Escherichia coli. J Bioenerg Biomembr 37:67–74
2. Bi Y, Watts JC, Bamford PK, Briere LK, Dunn SD (2008) Probing the functional tolerance of the b subunit of Escherichia coli ATP synthase for sequence manipulation through a chimera approach. Biochim Biophys Acta
3. Claggett SB, Grabar TB, Dunn SD, Cain BD (2007) Functional incorporation of chimeric b subunits into F1Fo ATP synthase. J Bacteriol 189:5463–5471
4. Del Rizzo PA, Bi Y, Dunn SD (2006) ATP synthase b subunit dimerization domain: a right-handed coiled coil with offset helices. J Mol Biol 364:735–746
5. Del Rizzo PA, Bi Y, Dunn SD, Shilton BH (2002) The “second stalk” of Escherichia coli ATP synthase: structure of the isolated dimerization domain. Biochemistry 41:6875–6884
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1. Energy Transduction by the Two Molecular Motors of the F1Fo ATP Synthase;Photosynthesis;2011-08-03
2. The b Subunits in the Peripheral Stalk of F1F0 ATP Synthase Preferentially Adopt an Offset Relationship;Journal of Biological Chemistry;2009-06
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