Low resolution structure of subunit b (b (22-156)) of Escherichia coli F(1)F(O) ATP synthase in solution and the b-delta assembly

Ragunathan Priya, Vikeramjeet S Tadwal, Manfred W Roessle, Shovanlal Gayen, Cornelia Hunke, Weng Chuan Peng, Jaume Torres, Gerhard Grüber

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)245-55
Number of pages11
JournalJournal of bioenergetics and biomembranes
Volume40
Issue number4
DOIs
Publication statusPublished - Aug 2008
Externally publishedYes

Keywords

  • Adenosine Triphosphate/chemistry
  • Bacterial Proton-Translocating ATPases/chemistry
  • Binding Sites
  • Computer Simulation
  • Enzyme Activation
  • Enzyme Stability
  • Escherichia coli/enzymology
  • Magnetic Resonance Spectroscopy
  • Models, Chemical
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Protein Subunits/chemistry

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