Secondary structure and 1H, 13C and 15N resonance assignments of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli

Biomol NMR Assign. 2010 Oct;4(2):179-81. doi: 10.1007/s12104-010-9236-7. Epub 2010 Jun 5.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins / chemistry*
  • Carbon Isotopes
  • Escherichia coli / chemistry*
  • Escherichia coli Proteins / chemistry*
  • Hydrogen
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Structure, Secondary

Substances

  • Bacterial Outer Membrane Proteins
  • BamE protein, E coli
  • Carbon Isotopes
  • Escherichia coli Proteins
  • Nitrogen Isotopes
  • Hydrogen