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Darobactin B stabilises a lateral-closed conformation of the BAM complex in E. coli cells
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dc.contributor.author | Haysom, Samuel F | |
dc.contributor.author | Machin, Jonathan | |
dc.contributor.author | Whitehouse, James M | |
dc.contributor.author | Horne, Jim E | |
dc.contributor.author | Fenn, Katherine | |
dc.contributor.author | Ma, Yue | |
dc.contributor.author | El Mkami, Hassane | |
dc.contributor.author | Böhringer, Nils | |
dc.contributor.author | Schäberle, Till F | |
dc.contributor.author | Ranson, Neil A | |
dc.contributor.author | Radford, Sheena E | |
dc.contributor.author | Pliotas, Christos | |
dc.date.accessioned | 2023-06-01T11:30:13Z | |
dc.date.available | 2023-06-01T11:30:13Z | |
dc.date.issued | 2023-08-21 | |
dc.identifier | 286200775 | |
dc.identifier | 3bfa8148-7ce5-4959-8eae-e2bbc266b11f | |
dc.identifier | 85160632625 | |
dc.identifier.citation | Haysom , S F , Machin , J , Whitehouse , J M , Horne , J E , Fenn , K , Ma , Y , El Mkami , H , Böhringer , N , Schäberle , T F , Ranson , N A , Radford , S E & Pliotas , C 2023 , ' Darobactin B stabilises a lateral-closed conformation of the BAM complex in E. coli cells ' , Angewandte Chemie International Edition , vol. 62 , no. 34 , e202218783 . https://doi.org/10.1002/anie.202218783 | en |
dc.identifier.issn | 1433-7851 | |
dc.identifier.other | RIS: urn:D6C2B91BCAB9D6AC88AEB8824FF8256E | |
dc.identifier.other | ORCID: /0000-0002-0552-5784/work/136288405 | |
dc.identifier.uri | https://hdl.handle.net/10023/27725 | |
dc.description | Funding: C.P. acknowledges the Biotechnology and Biological Sciences Research Council (BBSRC) (BB/S018069/1; BB/W019795/1) for funding. cwEPR data were collected at the Pliotas Laboratory (BB/S018069/1) and PELDOR data were collected at the University of St Andrews, supported by equipment funding from the Wellcome Trust (WT) (099149/Z/12/Z) and BBSRC (BB/R013780/1). CryoEM data were collected at the Astbury Biostructure Laboratory, funded by the University of Leeds and the WT (108466/Z/15/Z; 221524/Z/20/Z). J.E.H. and K.F. acknowledge funding from the Medical Research Council (MRC) (MR/P018491/1). S.F.H. is funded by the White Rose BBSRC DTP (BB/M011151/1). J.M. is funded by the WT (222373/Z/21/Z). SER holds a Royal Society Professorial Fellowship (RSRP/R1/211057). T.F.S and N.B. acknowledge funding from the German Federal Ministry of Education and Research (BMBF, via grant GBi2S and German Centrefor Infection Research (DZIF) 09.918). | en |
dc.description.abstract | The Β-barrel assembly machinery (BAM complex) is essential for outer membrane protein (OMP) folding in Gram-negative bacteria, and represents a promising antimicrobial target. Several conformational states of BAM have been reported, but all have been obtained under conditions which lack the unique features and complexity of the outer membrane (OM). Here, we use Pulsed Electron-Electron Double Resonance (PELDOR, or DEER) spectroscopy distance measurements to interrogate the conformational ensemble of the BAM complex in E. coli cells. We show that BAM adopts a broad ensemble of conformations in the OM, while in the presence of the antibiotic darobactin B (DAR-B), BAM's conformational equilibrium shifts to a restricted ensemble consistent with the lateral closed state. Our in-cell PELDOR findings are supported by new cryoEM structures of BAM in the presence and absence of DAR-B. This work demonstrates the utility of PELDOR to map conformational changes in BAM within its native cellular environment. | |
dc.format.extent | 8 | |
dc.format.extent | 608261 | |
dc.language.iso | eng | |
dc.relation.ispartof | Angewandte Chemie International Edition | en |
dc.subject | PELDOR | en |
dc.subject | BAM | en |
dc.subject | Darobactin | en |
dc.subject | In-cell EPR | en |
dc.subject | CryoEM | en |
dc.subject | NDAS | en |
dc.subject | MCC | en |
dc.title | Darobactin B stabilises a lateral-closed conformation of the BAM complex in E. coli cells | en |
dc.type | Journal article | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.contributor.sponsor | BBSRC | en |
dc.contributor.institution | University of St Andrews. School of Physics and Astronomy | en |
dc.identifier.doi | https://doi.org/10.1002/anie.202218783 | |
dc.description.status | Peer reviewed | en |
dc.identifier.grantnumber | 099149/Z/12/Z | en |
dc.identifier.grantnumber | BB/R013780/1 | en |
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