title: 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.
abstract: 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.
authors.affiliation: School of Cancer Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. t.j.knowles@bham.ac.uk
authors.forename: Timothy J
authors.initials: TJ
authors.lastname: Knowles
authors.forename: Darren M
authors.initials: DM
authors.lastname: McClelland
authors.forename: Sandya
authors.initials: S
authors.lastname: Rajesh
authors.forename: Ian R
authors.initials: IR
authors.lastname: Henderson
authors.forename: Michael
authors.initials: M
authors.lastname: Overduin
mesh_terms: 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
chemical_list: D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins