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Article
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
Abstract
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
Disciplines
Publication Date
August 5, 2011
DOI
10.1016/j.jmb.2011.05.022
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
Available at: http://works.bepress.com/lisa-warner/14/