Secondary structure and (1)H, (13)C and (15)N backbone resonance assignments of BamC, a component of the outer membrane protein assembly machinery in Escherichia coli.
We report the (1)H, (13)C and (15)N backbone chemical shift assignments and secondary structure of the Escherichia coli protein BamC, a 32-kDa protein subunit that forms part of the BAM (Omp85) complex, the beta-barrel assembly machinery present in all Gram-negative bacteria and which is essential for viability.
Knowles
Timothy J
TJ
School of Cancer Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. t.j.knowles@bham.ac.uk
McClelland
Darren M
DM
Rajesh
Sandya
S
Henderson
Ian R
IR
Overduin
Michael
M
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins