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TitlePlasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 7131, Year 2021
Publish dateDec 8, 2021
AuthorsRunrun Wu / Jeremy W Bakelar / Karl Lundquist / Zijian Zhang / Katie M Kuo / David Ryoo / Yui Tik Pang / Chen Sun / Tommi White / Thomas Klose / Wen Jiang / James C Gumbart / Nicholas Noinaj /
PubMed AbstractIn Gram-negative bacteria, the biogenesis of β-barrel outer membrane proteins is mediated by the β-barrel assembly machinery (BAM). The mechanism employed by BAM is complex and so far- incompletely ...In Gram-negative bacteria, the biogenesis of β-barrel outer membrane proteins is mediated by the β-barrel assembly machinery (BAM). The mechanism employed by BAM is complex and so far- incompletely understood. Here, we report the structures of BAM in nanodiscs, prepared using polar lipids and native membranes, where we observe an outward-open state. Mutations in the barrel domain of BamA reveal that plasticity in BAM is essential, particularly along the lateral seam of the barrel domain, which is further supported by molecular dynamics simulations that show conformational dynamics in BAM are modulated by the accessory proteins. We also report the structure of BAM in complex with EspP, which reveals an early folding intermediate where EspP threads from the underside of BAM and incorporates into the barrel domain of BamA, supporting a hybrid-barrel budding mechanism in which the substrate is folded into the membrane sequentially rather than as a single unit.
External linksNat Commun / PubMed:34880256 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 8.0 Å
Structure data

24473

7ri4

EMDB-24473, PDB-7ri4:
Structure of a BAM/EspP(beta9-12) hybrid-barrel intermediate
Method: EM (single particle) / Resolution: 3.4 Å

24474

7ri5

EMDB-24474, PDB-7ri5:
Structure of a BAM in MSP1E3D1 nanodiscs at 4 Angstrom resolution
Method: EM (single particle) / Resolution: 4.0 Å

24475

7ri6

EMDB-24475, PDB-7ri6:
Structure of BAM in MSP1E3D1 nanodiscs prepared from E. coli outer membranes
Method: EM (single particle) / Resolution: 5.9 Å

24476

7ri7

EMDB-24476, PDB-7ri7:
The structure of BAM in MSP1D1 nanodiscs
Method: EM (single particle) / Resolution: 8.0 Å

24477

7ri8

EMDB-24477, PDB-7ri8:
The structure of BAM in MSP2N2 nanodiscs
Method: EM (single particle) / Resolution: 7.5 Å

24478

7ri9

EMDB-24478, PDB-7ri9:
The structure of BAM in MSP1E3D1 at 6.9 Angstrom resolution
Method: EM (single particle) / Resolution: 6.9 Å

24481

7rj5

EMDB-24481, PDB-7rj5:
The structure of BAM in complex with EspP at 7 Angstrom resolution
Method: EM (single particle) / Resolution: 7.0 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • escherichia coli (E. coli)
KeywordsMEMBRANE PROTEIN / BAM / EspP / hybrid barrel / native membrane

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