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J Mol Biol. 2011 Aug 5;411(1):83-95. doi: 10.1016/j.jmb.2011.05.022. Epub 2011 May 23.

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

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  • 1Department of Chemistry and Biochemistry, University of Colorado, Boulder, Boulder, CO 80309, USA.

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 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.

Copyright © 2011 Elsevier Ltd. All rights reserved.

PMID:
21624375
[PubMed - indexed for MEDLINE]
PMCID:
PMC3182476
Free PMC Article

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