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TitleStructural insights into outer membrane protein biogenesis in pathogenic Neisseria.
Journal, issue, pagesStructure, Vol. 33, Issue 11, Page 1893-11903.e3, Year 2025
Publish dateNov 6, 2025
AuthorsEvan Billings / Zixing Fan / Moloud Aflaki Sooreshjani / James C Gumbart / Nicholas Noinaj /
PubMed AbstractN. gonorrhoeae (Ngo) causes the sexually transmitted infection gonorrhea with ∼106 million infections worldwide annually. Ngo infections can result in an increased risk of acquiring HIV, ...N. gonorrhoeae (Ngo) causes the sexually transmitted infection gonorrhea with ∼106 million infections worldwide annually. Ngo infections can result in an increased risk of acquiring HIV, infertility, and blindness. To combat Ngo infections, we report the cryoelectron microscopy (cryo-EM) structure of the Ngo β-barrel assembly machinery (NgBAM), which is responsible for the biogenesis of β-barrel outer membrane proteins (OMPs). NgBAM was observed in an inward-open state; however, the polypeptide transport-associated (POTRA) domains more closely match those found in the outward-open state in E. coli β-barrel assembly machinery (BAM). The barrel seam of NgBamA consists of partial pairing of strand β1 with β16; no outward-open state of NgBAM was observed. Molecular dynamics (MD) simulations reveal unique overall dynamics and interplay between the POTRA domains of NgBamA and NgBamD. We propose that in Ngo, initial recognition occurs in the inward-open state where the last strand of the OMP partially pairs with β1 of NgBamA and must compete off β16.
External linksStructure / PubMed:40902586 / PubMed Central
MethodsEM (single particle)
Resolution4.0 - 6.3 Å
Structure data

45754

9cmw

EMDB-45754, PDB-9cmw:
The cryo-EM structure of BamACDE complex from Neisseria gonorrhoeae
Method: EM (single particle) / Resolution: 4.0 Å

45755

9cn0

EMDB-45755, PDB-9cn0:
The cryo-EM structure of BamADE subcomplex from Neisseria gonorrhoeae
Method: EM (single particle) / Resolution: 6.3 Å

45756

9cn1

EMDB-45756, PDB-9cn1:
The cryo-EM structure of BamAD subcomplex from Neisseria gonorrhoeae
Method: EM (single particle) / Resolution: 5.0 Å

Source
  • neisseria gonorrhoeae (bacteria)
  • neisseria gonorrhoeae fa 1090 (bacteria)
KeywordsMEMBRANE PROTEIN / beta barrel assembly machinery / BAM complex / outer membrane protein / Neisseria / Neisseria gonnorhoeae / protein folding / beta barrel membrane protein

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