Structure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data Set.
Structure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data Set.
J Mol Biol. 2011 May 23;
Authors: Warner LR, Varga K, Lange OF, Baker SL, Baker D, Sousa MC, Pardi A
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 ?-barrel assembly machine in E. coli. The first 100 residues in BamC were disordered in solution. The Rosetta calculations showed that BamC(101-344) 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. (15)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.
PMID: 21624375 [PubMed - as supplied by publisher]
Source:
PubMed