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Structure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data Set
Journal of Molecular Biology (2011)
  • Lisa R. Warner, University of Colorado, Boulder
  • Krisztina Varga, University of Colorado, Boulder
  • Oliver F. Lange, University of Washington
  • Susan Baker, University of Colorado, Boulder
  • David Baker, University of Washington
  • Marcelo C. Sousa, University of Colorado, Boulder
  • Arthur Pardi, University of Washington
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 BamC<sub>101–344</sub> 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. <sup>15</sup>N 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
Publication Date
August 5, 2011
Citation Information
Lisa R. Warner, Krisztina Varga, Oliver F. Lange, Susan Baker, et al.. "Structure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data Set" Journal of Molecular Biology Vol. 411 Iss. 1 (2011) p. 83 - 95
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