Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set.

Academic Article


  • The CS-RDC-NOE Rosetta program was used to generate the solution structure of a 27-kDa fragment of the Escherichia coli BamC protein from a limited set of NMR data. The BamC protein is a component of the essential five-protein β-barrel assembly machine in E. coli. The first 100 residues in BamC were disordered in solution. The Rosetta calculations showed that BamC₁₀₁₋₃₄₄ forms two well-defined domains connected by an ~18-residue linker, where the relative orientation of the domains was not defined. Both domains adopt a helix-grip fold previously observed in the Bet v 1 superfamily. ¹⁵N relaxation data indicated a high degree of conformational flexibility for the linker connecting the N-terminal domain and the C-terminal domain in BamC. The results here show that CS-RDC-NOE Rosetta is robust and has a high tolerance for misassigned nuclear Overhauser effect restraints, greatly simplifying NMR structure determinations.
  • Authors

  • Warner, Lisa R
  • Varga, Krisztina
  • Lange, Oliver F
  • Baker, Susan L
  • Baker, David
  • Sousa, Marcelo C
  • Pardi, Arthur
  • Status

    Publication Date

  • August 5, 2011
  • Published In


  • Computational Biology
  • Escherichia coli
  • Escherichia coli Proteins
  • Lipid-Linked Proteins
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Protein Folding
  • Software
  • Digital Object Identifier (doi)

    Start Page

  • 83
  • End Page

  • 95
  • Volume

  • 411
  • Issue

  • 1