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Published online before print August 31, 2007, 10.1110/ps.072776307
Protein Science (2007), 16:2118-2122. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c

Oleg Y. Dmitriev1 and Robert H. Fillingame2

1 Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5, Canada
2 Department of Biomolecular Chemistry, University of Wisconsin–Madison, Madison, Wisconsin 53706, USA

(RECEIVED January 16, 2007; FINAL REVISION June 12, 2007; ACCEPTED June 12, 2007)

We have tested the role of the polar loop of subunit c of the Escherichia coli ATP synthase in stabilizing the hairpin structure of this protein. The structure of the c32–52 peptide corresponding to the cytoplasmic region of subunit c bound to the dodecylphosphocholine micelles was solved by high-resolution NMR. The region comprising residues 41–47 forms a well-ordered structure rather similar to the conformation of the polar loop region in the solution structure of the full-length subunit c and is flanked by short {alpha}-helical segments. This result suggests that the rigidity of the polar loop significantly contributes to the stability of the hairpin formed by the two helices of subunit c. This experimental system may be useful for NMR studies of interactions between subunit c and subunits {gamma} and {varepsilon}, which together form the rotor of the ATP synthase.

Keywords: ATP synthase; protein NMR; peptide structure; membrane protein


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