{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hagan CL"],"funding":["HHS | NIH | National Institute of General Medical Sciences","NIAID NIH HHS","NIGMS NIH HHS"],"pagination":["2011-6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4343090"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["112(7)"],"pubmed_abstract":["The protein complex that assembles integral membrane β-barrel proteins in the outer membranes of Gram-negative bacteria is an attractive target in the development of new antibiotics. This complex, the β-barrel assembly machine (Bam), contains two essential proteins, BamA and BamD. We have identified a peptide that inhibits the assembly of β-barrel proteins in vitro by characterizing the interaction of BamD with an unfolded substrate protein. This peptide is a fragment of the substrate protein and contains a conserved amino acid sequence. We have demonstrated that mutations of this sequence in the full-length substrate protein impair the protein's assembly, implying that BamD's interaction with this sequence is an important part of the assembly mechanism. Finally, we have found that in vivo"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Inhibition of the β-barrel assembly machine by a peptide that binds BamD."],"pmcid":["PMC4343090"],"funding_grant_id":["F32GM108258","F32 GM108258","AI081059","R01 AI081059"],"pubmed_authors":["Wzorek JS","Hagan CL","Kahne D"],"additional_accession":[]},"is_claimable":false,"name":"Inhibition of the β-barrel assembly machine by a peptide that binds BamD.","description":"The protein complex that assembles integral membrane β-barrel proteins in the outer membranes of Gram-negative bacteria is an attractive target in the development of new antibiotics. This complex, the β-barrel assembly machine (Bam), contains two essential proteins, BamA and BamD. We have identified a peptide that inhibits the assembly of β-barrel proteins in vitro by characterizing the interaction of BamD with an unfolded substrate protein. This peptide is a fragment of the substrate protein and contains a conserved amino acid sequence. We have demonstrated that mutations of this sequence in the full-length substrate protein impair the protein's assembly, implying that BamD's interaction with this sequence is an important part of the assembly mechanism. Finally, we have found that in vivo","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Feb","modification":"2026-05-02T21:17:29.829Z","creation":"2026-04-07T18:31:35.258Z"},"accession":"S-EPMC4343090","cross_references":{"pubmed":["25646443"],"doi":["10.1073/pnas.1415955112"]}}