| Literature DB >> 18668355 |
Ragunathan Priya1, Vikeramjeet S Tadwal, Manfred W Roessle, Shovanlal Gayen, Cornelia Hunke, Weng Chuan Peng, Jaume Torres, Gerhard Grüber.
Abstract
The first low resolution solution structure of the soluble domain of subunit b (b (22-156)) of the Escherichia coli F(1)F(O) ATPsynthase was determined from small-angle X-ray scattering data. The dimeric protein has a boomerang-like shape with a total length of 16.2 +/- 0.3 nm. Fluorescence correlation spectroscopy (FCS) shows that the protein binds effectively to the subunit delta, confirming their described neighborhood. Using the recombinant C-terminal domain (delta(91-177)) of subunit delta and the C-terminal peptides of subunit b, b (120-140) and b (140-156), FCS titration experiments were performed to assign the segments involved in delta-b assembly. These data identify the very C-terminal tail b (140-156) to interact with delta(91-177). The novel 3D structure of this peptide has been determined by NMR spectroscopy. The molecule adopts a stable helix formation in solution with a flexible tail between amino acid 140 to 145.Entities:
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Year: 2008 PMID： 18668355 DOI： 10.1007/s10863-008-9154-x
Source DB: PubMed Journal: J Bioenerg Biomembr ISSN： 0145-479X Impact factor: 3.853