Structure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data Set
2011
Warner, Lisa R. | Varga, Krisztina | Lange, Oliver F. | Baker, Susan L. | Baker, David | Sousa, Marcelo C. | Pardi, Arthur
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.
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