Crossref journal-article
Wiley
Protein Science (311)
Abstract

AbstractWe 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 α‐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 γ and ε, which together form the rotor of the ATP synthase.

Bibliography

Dmitriev, O. Y., & Fillingame, R. H. (2007). The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c. Protein Science, 16(10), 2118–2122. Portico.

Authors 2
  1. Oleg Y. Dmitriev (first)
  2. Robert H. Fillingame (additional)
Dates
Type When
Created 18 years ago (Aug. 31, 2007, 8:44 p.m.)
Deposited 1 year, 11 months ago (Sept. 28, 2023, 10 p.m.)
Indexed 1 year ago (Aug. 10, 2024, 1:11 a.m.)
Issued 17 years, 11 months ago (Oct. 1, 2007)
Published 17 years, 11 months ago (Oct. 1, 2007)
Published Online 16 years, 8 months ago (Jan. 1, 2009)
Published Print 17 years, 11 months ago (Oct. 1, 2007)
Funders 0

None

@article{Dmitriev_2007, title={The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c}, volume={16}, ISSN={1469-896X}, url={http://dx.doi.org/10.1110/ps.072776307}, DOI={10.1110/ps.072776307}, number={10}, journal={Protein Science}, publisher={Wiley}, author={Dmitriev, Oleg Y. and Fillingame, Robert H.}, year={2007}, month=oct, pages={2118–2122} }