Structure of a bacterial membrane chaperone complex


The proteins of the outer membrane of Gram-negative bacteria are critical for bacterial survival. The understanding of how these proteins are targeted and folded into this membrane is critical as it could offer significant medical benefits. Compounds that inhibit key stages of this process could prove useful in combating diverse Gram negative pathogens. The core complex, known as the beta-barrel assembly machinery (Bam), is composed of five proteins in E. coli, an integral membrane protein, BamA, and four periplasmically located lipoproteins, BamB-E. The individual structures of the isolated Bam proteins are now known but the way in which these components interact and form the functional Bam complex is not. In this experiment we will use contrast variation SANS to determine the overall structure of the BamCDE complex.

Metadata Access
Creator Dr Cameron Neylon; Dr Luke Clifton; Dr Tim Knowles; Dr Mark Jeeves
Publisher ISIS Neutron and Muon Source
Publication Year 2015
Rights CC-BY Attribution 4.0 International;
OpenAccess true
Contact isisdata(at)
Resource Type Dataset
Discipline Photon- and Neutron Geosciences
Temporal Coverage Begin 2012-10-30T08:49:49Z
Temporal Coverage End 2012-11-01T16:28:16Z