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TitleThe role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 4174, Year 2021
Publish dateJul 7, 2021
AuthorsPaul 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 AbstractThe 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 linksNat Commun / PubMed:34234105 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.95 - 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
KeywordsIMMUNE SYSTEM / Antibody / antibiotic / Fab / BamA / MEMBRANE PROTEIN / Outer membrane protein assembly / beta-barrel / Gram negative bacteria / protein foldase

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