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Structure paper

TitleStructure of a distinct β-barrel assembly machinery complex in the Bacteroidota.
Journal, issue, pagesNat Microbiol, Vol. 10, Issue 11, Page 2845-2859, Year 2025
Publish dateOct 1, 2025
AuthorsAugustinas Silale / Mariusz Madej / Katarzyna Mikruta / Andrew M Frey / Adam J Hart / Arnaud Baslé / Carsten Scavenius / Jan J Enghild / Matthias Trost / Robert P Hirt / Bert van den Berg /
PubMed AbstractThe Gram-negative β-barrel assembly machinery (BAM) complex catalyses the folding and membrane insertion of newly synthesized β-barrel outer membrane proteins. The BAM is structurally conserved, ...The Gram-negative β-barrel assembly machinery (BAM) complex catalyses the folding and membrane insertion of newly synthesized β-barrel outer membrane proteins. The BAM is structurally conserved, but most studies have focused on Gammaproteobacteria. Here, using single-particle cryogenic electron microscopy, quantitative proteomics and functional assays, we show that the BAM complex is distinct within the Bacteroidota. Cryogenic electron microscopy structures of BAM complexes from the human gut symbiont Bacteroides thetaiotaomicron (3.3 Å) and the human oral pathogen Porphyromonas gingivalis (3.2 Å) show similar, seven-component complexes of ~325 kDa. The complexes are mostly extracellular and comprise canonical BamA and BamD; an integral, essential outer membrane protein, BamG, that associates with BamA; and four surface-exposed lipoproteins: BamH-K. Absent from the BAM in Pseudomonadota, BamG-K form a large, extracellular dome that may confer additional functionality to enable the folding and assembly of β-barrel-surface-exposed lipoprotein complexes that are a hallmark of the Bacteroidota. Our findings develop our understanding of fundamental biological processes in an important bacterial phylum.
External linksNat Microbiol / PubMed:41034344 / PubMed Central
MethodsEM (single particle)
Resolution3.24 - 4.26 Å
Structure data

52200

9his

EMDB-52200, PDB-9his:
Extracellular components BamHIJK of the Bacteroides thetaiotaomicron BAM machinery
Method: EM (single particle) / Resolution: 3.28 Å

52202

9hiv

EMDB-52202, PDB-9hiv:
BamADG components of the Bacteroides thetaiotaomicron BAM machinery
Method: EM (single particle) / Resolution: 3.46 Å

52209

9hj3

EMDB-52209, PDB-9hj3:
Bacteroides thetaiotaomicron BAM complex
Method: EM (single particle) / Resolution: 3.46 Å

52218

9hjm

EMDB-52218, PDB-9hjm:
Porphyromonas gingivalis BAM complex
Method: EM (single particle) / Resolution: 3.24 Å

EMDB-52219: Porphyromonas gingivalis BAM complex with periplasmic density
Method: EM (single particle) / Resolution: 4.26 Å

Chemicals

ChemComp-TDA:
N-TRIDECANOIC ACID

ChemComp-Z41:
(2S)-3-hydroxypropane-1,2-diyl dihexadecanoate

ChemComp-PLM:
PALMITIC ACID

Source
  • bacteroides thetaiotaomicron vpi-5482 (bacteria)
  • porphyromonas gingivalis atcc 33277 (bacteria)
KeywordsMEMBRANE PROTEIN / Lipoproteins / Outer membrane protein biogenesis / Beta-barrel assembly machinery / BAM / Outer membrane biogenesis / Gram-negative bacteria

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