Structure and function of BamE within the outer membrane and the β-barrel assembly machine

Timothy J Knowles, Douglas F Browning, Mark Jeeves, Riyaz Maderbocus, Sandya Rajesh, Pooja Sridhar, Eleni Manoli, Danielle Emery, Ulf Sommer, Ashley Spencer, Denisse L Leyton, Derrick Squire, Roy R Chaudhuri, Mark R Viant, Adam F Cunningham, Ian R Henderson, Michael Overduin

Research output: Contribution to journalArticlepeer-review


Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential β-barrel assembly machine (Bam). Here, we report the native structure and mechanism of a core component of this complex, BamE, and show that it is exclusively monomeric in its native environment of the periplasm, but is able to adopt a distinct dimeric conformation in the cytoplasm. BamE is shown to bind specifically to phosphatidylglycerol, and comprehensive mutagenesis and interaction studies have mapped key determinants for complex binding, outer membrane integrity and cell viability, as well as revealing the role of BamE within the Bam complex.

Original languageEnglish
Pages (from-to)123-128
Number of pages6
JournalEmbo Reports
Issue number2
Publication statusPublished - Feb 2011


  • Bacterial Outer Membrane Proteins/chemistry
  • Binding Sites
  • Escherichia coli Proteins/chemistry
  • Magnetic Resonance Spectroscopy
  • Mutagenesis, Site-Directed
  • Mutant Proteins/chemistry
  • Periplasmic Proteins/chemistry
  • Phosphatidylglycerols/chemistry
  • Protein Binding
  • Protein Conformation
  • Recombinant Proteins/chemistry


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