Secondary structure and 1H, 13C and 15N resonance assignments of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli.
We report the (1)H, (13)C and (15)N backbone and side chain chemical shift assignments and secondary structure of the Escherichia coli protein BamE, a subunit of the BAM (Omp85) complex, the β-barrel assembly machinery present in all Gram-negative bacteria, mitochondria and chloroplasts and is essential for viability.
School of Cancer Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. t.j.knowles@bham.ac.uk
Timothy J
TJ
Knowles
Pooja
P
Sridhar
Sandya
S
Rajesh
Eleni
E
Manoli
Michael
M
Overduin
Ian R
IR
Henderson
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D002247:Carbon Isotopes; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006859:Hydrogen; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary
D001425:Bacterial Outer Membrane Proteins; C523551:BamE protein, E coli; D002247:Carbon Isotopes; D029968:Escherichia coli Proteins; D009587:Nitrogen Isotopes; D006859:Hydrogen