2LAF: NMR solution structure of the N-terminal domain of the E. coli lipoprotein BamC

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 beta-barrel assembly machine in E. coli. The first 100 residues in BamC were disordered in solution. The Rosetta calculations showed that BamC(1)(0)(1)(-)(3)(4)(4) 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. (1)(5)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.
PDB ID: 2LAFDownload
MMDB ID: 138652
PDB Deposition Date: 2011/3/11
Updated in MMDB: 2018/05
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2LAF: monomeric; determined by author
Molecular Components in 2LAF
Label Count Molecule
Protein (1 molecule)
Lipoprotein 34(Gene symbol: bamC)
Molecule annotation
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Citing MMDB