Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
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Journal
IF	>30 >20 >10 >5 all

Title	The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding.
Journal, issue, pages	Nat Commun, Vol. 12, Issue 1, Page 4174, Year 2021
Publish date	Jul 7, 2021
Authors	Paul White / Samuel F Haysom / Matthew G Iadanza / Anna J Higgins / Jonathan M Machin / James M Whitehouse / Jim E Horne / Bob Schiffrin / Charlotte Carpenter-Platt / Antonio N Calabrese / Kelly M Storek / Steven T Rutherford / David J Brockwell / Neil A Ranson / Sheena E Radford /
PubMed Abstract	The folding of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria is catalysed by the β-barrel assembly machinery (BAM). How lateral opening in the β-barrel of the major subunit ...The folding of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria is catalysed by the β-barrel assembly machinery (BAM). How lateral opening in the β-barrel of the major subunit BamA assists in OMP folding, and the contribution of membrane disruption to BAM catalysis remain unresolved. Here, we use an anti-BamA monoclonal antibody fragment (Fab1) and two disulphide-crosslinked BAM variants (lid-locked (LL), and POTRA-5-locked (P5L)) to dissect these roles. Despite being lethal in vivo, we show that all complexes catalyse folding in vitro, albeit less efficiently than wild-type BAM. CryoEM reveals that while Fab1 and BAM-P5L trap an open-barrel state, BAM-LL contains a mixture of closed and contorted, partially-open structures. Finally, all three complexes globally destabilise the lipid bilayer, while BamA does not, revealing that the BAM lipoproteins are required for this function. Together the results provide insights into the role of BAM structure and lipid dynamics in OMP folding.
External links	Nat Commun / PubMed:34234105 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	2.95 - 10.3 Å
Structure data	12232 7bnq EMDB-12232, PDB-7bnq: Lateral-closed conformation of the lid-locked BAM complex (BamA E435C S665C, BamBDCE) by cryoEM Method: EM (single particle) / Resolution: 4.1 Å 12262 7nbx EMDB-12262, PDB-7nbx: Lateral-open conformation of the lid-locked BAM complex (BamA E435C S665C, BamBDCE) by cryoEM Method: EM (single particle) / Resolution: 4.8 Å EMDB-12263: structure of a POTRA-locked BAM complex in a lateral-open conformation Method: EM (single particle) / Resolution: 10.3 Å 12271 7ncs EMDB-12271, PDB-7ncs: Lateral-open conformation of the lid-locked BAM complex (BamA E435C S665C, BamBDCE) bound by a bactericidal Fab fragment Method: EM (single particle) / Resolution: 7.1 Å 12272 7nd0 EMDB-12272, PDB-7nd0: lateral-open conformation of the wild-type BAM complex (BamABCDE) bound to a bactericidal Fab fragment Method: EM (single particle) / Resolution: 5.2 Å PDB-7bm5: Crystal structure of Fab1, the Fab fragment of the anti-BamA monoclonal antibody MAB1 Method: X-RAY DIFFRACTION / Resolution: 2.95 Å
Source	escherichia coli (strain k12) (bacteria) escherichia coli k-12 (bacteria) homo sapiens (human) Escherichia coli K-12
Keywords	IMMUNE SYSTEM / Antibody / antibiotic / Fab / BamA / MEMBRANE PROTEIN / Outer membrane protein assembly / beta-barrel / Gram negative bacteria / protein foldase