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TitleStructural basis of BAM-mediated outer membrane β-barrel protein assembly.
Journal, issue, pagesNature, Vol. 617, Issue 7959, Page 185-193, Year 2023
Publish dateApr 26, 2023
AuthorsChongrong Shen / Shenghai Chang / Qinghua Luo / Kevin Chun Chan / Zhibo Zhang / Bingnan Luo / Teng Xie / Guangwen Lu / Xiaofeng Zhu / Xiawei Wei / Changjiang Dong / Ruhong Zhou / Xing Zhang / Xiaodi Tang / Haohao Dong /
PubMed AbstractThe outer membrane structure is common in Gram-negative bacteria, mitochondria and chloroplasts, and contains outer membrane β-barrel proteins (OMPs) that are essential interchange portals of ...The outer membrane structure is common in Gram-negative bacteria, mitochondria and chloroplasts, and contains outer membrane β-barrel proteins (OMPs) that are essential interchange portals of materials. All known OMPs share the antiparallel β-strand topology, implicating a common evolutionary origin and conserved folding mechanism. Models have been proposed for bacterial β-barrel assembly machinery (BAM) to initiate OMP folding; however, mechanisms by which BAM proceeds to complete OMP assembly remain unclear. Here we report intermediate structures of BAM assembling an OMP substrate, EspP, demonstrating sequential conformational dynamics of BAM during the late stages of OMP assembly, which is further supported by molecular dynamics simulations. Mutagenic in vitro and in vivo assembly assays reveal functional residues of BamA and EspP for barrel hybridization, closure and release. Our work provides novel insights into the common mechanism of OMP assembly.
External linksNature / PubMed:37100902
MethodsEM (single particle)
Resolution3.1 - 3.5 Å
Structure data

16137

8bnz

EMDB-16137, PDB-8bnz:
BAM-EspP complex structure with BamA-G431C/EspP-N1293C mutations in nanodisc
Method: EM (single particle) / Resolution: 3.5 Å

16138

8bo2

EMDB-16138, PDB-8bo2:
BAM-EspP complex structure with BamA-S425C/EspP-S1299C mutations in nanodisc
Method: EM (single particle) / Resolution: 3.1 Å

33763

7ye4

EMDB-33763, PDB-7ye4:
BAM-EspP complex structure with BamA-G431C and G781C/EspP-N1293C and A1043C mutations in nanodisc
Method: EM (single particle) / Resolution: 3.4 Å

33765

7ye6

EMDB-33765, PDB-7ye6:
BAM-EspP complex structure with BamA-N427C/EspP-R1297C mutations in nanodisc
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • escherichia coli k-12 (bacteria)
  • escherichia coli o157:h7 (bacteria)
KeywordsMEMBRANE PROTEIN / BAM / BamABCDE / EspP / Gram-negative bacteria / outer membrane protein / outer membrane barrel / BamA / BamB / BamC / BamD / BamE / TRANSPORT PROTEIN / Outer membrane protein insertion and release

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