{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Webb CT"],"funding":["Intramural NIH HHS","NHMRC Postgraduate Research Scholarship","Intramural Research Program of the National Institutes of Health, National Institute of Diabetes and Digestive and Kidney Diseases","National Health and Medical Research Council (NHMRC) of Australia"],"pagination":["545-55"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3433275"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["422(4)"],"pubmed_abstract":["The β-barrel assembly machinery (BAM) complex drives the assembly of β-barrel proteins into the outer membrane of gram-negative bacteria. It is composed of five subunits: BamA, BamB, BamC, BamD, and BamE. We find that the BAM complex isolated from the outer membrane of Escherichia coli consists of a core complex of BamA:B:C:D:E and, in addition, a BamA:B module and a BamC:D module. In the absence of BamC, these modules are destabilized, resulting in increased protease susceptibility of BamD and BamB. While the N-terminus of BamC carries a highly conserved region crucial for stable interaction with BamD, immunofluorescence, immunoprecipitation, and protease-sensitivity assays show that the C-terminal domain of BamC, composed of two helix-grip motifs, is exposed on the surface of E. coli. Th"],"journal":["Journal of molecular biology"],"pubmed_title":["Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC."],"pmcid":["PMC3433275"],"funding_grant_id":["606788","ZIA DK036139-05"],"pubmed_authors":["Buchanan SK","Lithgow T","Webb CT","Noinaj N","Selkrig J","Perry AJ"],"additional_accession":[]},"is_claimable":false,"name":"Dynamic association of BAM complex modules includes surface exposure of the lipoprotein BamC.","description":"The β-barrel assembly machinery (BAM) complex drives the assembly of β-barrel proteins into the outer membrane of gram-negative bacteria. It is composed of five subunits: BamA, BamB, BamC, BamD, and BamE. We find that the BAM complex isolated from the outer membrane of Escherichia coli consists of a core complex of BamA:B:C:D:E and, in addition, a BamA:B module and a BamC:D module. In the absence of BamC, these modules are destabilized, resulting in increased protease susceptibility of BamD and BamB. While the N-terminus of BamC carries a highly conserved region crucial for stable interaction with BamD, immunofluorescence, immunoprecipitation, and protease-sensitivity assays show that the C-terminal domain of BamC, composed of two helix-grip motifs, is exposed on the surface of E. coli. Th","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Sep","modification":"2025-04-18T16:58:39.066Z","creation":"2019-03-27T00:57:26Z"},"accession":"S-EPMC3433275","cross_references":{"pubmed":["22683355"],"doi":["10.1016/j.jmb.2012.05.035"]}}