TY - JOUR
T1 - Escherichia coli F1Fo-ATP Synthase with a b/δ fusion protein allows analysis of the function of the individual b subunits
AU - Gajadeera, Chathurada S.
AU - Weber, Joachim
PY - 2013/9/13
Y1 - 2013/9/13
N2 - Background: The essential "stator stalk" connects the nonrotating portions of F1Fo-ATP synthase. Results: A b/δ fusion protein is functional and allows analyzing the role of the individual b subunits. Conclusion: One of the b subunits is required for binding to F 1, the other for binding to Fo. Significance: Understanding the function of the stator stalk is important for understanding the mechanism of ATP synthase.
AB - Background: The essential "stator stalk" connects the nonrotating portions of F1Fo-ATP synthase. Results: A b/δ fusion protein is functional and allows analyzing the role of the individual b subunits. Conclusion: One of the b subunits is required for binding to F 1, the other for binding to Fo. Significance: Understanding the function of the stator stalk is important for understanding the mechanism of ATP synthase.
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U2 - 10.1074/jbc.M113.503722
DO - 10.1074/jbc.M113.503722
M3 - Article
C2 - 23893411
AN - SCOPUS:84884196742
SN - 0021-9258
VL - 288
SP - 26441
EP - 26447
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 37
ER -