9N2E

Cryo-EM structure of F. johnsoniae BamAP

9N2E の概要

• エントリーDOI: 10.2210/pdb9n2e/pdb
• EMDBエントリー: 48836
• 分子名称: Surface antigen (D15), CarboxypepD_reg-like domain-containing protein (2 entities in total)
• 機能のキーワード: bamap complex, bama, bamp, outer-membrane proteins, omp, membrane protein
• 由来する生物種: Flavobacterium johnsoniae UW101; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 129904.06

構造登録者

Deme, J.C.,Lea, S.M. (登録日: 2025-01-28, 公開日: 2025-07-09, 最終更新日: 2026-01-21)

主引用文献

Liu, X.,Avramova, M.,Deme, J.C.,Jones, R.L.,Lundgren, C.A.K.,Lea, S.M.,Berks, B.C.
A shared mechanism for Bacteroidota protein transport and gliding motility.
Nat Commun, 16:10217-10217, 2025

PubMed Abstract: Bacteria of the phylum Bacteroidota are major human commensals and pathogens in addition to being abundant members of the wider biosphere. Bacteroidota move by gliding and they export proteins using the Type 9 Secretion System (T9SS). Here we discover that gliding motility and the T9SS share an unprecedented mechanism of energisation in which outer membrane proteins are covalently attached by disulfide bonds to a moving internal track structure that propels them laterally through the membrane. We determined the structure of an exemplar Bacteroidota mobile track by obtaining the cryoEM structure of a 3 MDa circular mini-track from Porphyromonas gingivalis. Our discoveries identify a mechanistic and evolutionary link between gliding motility and T9SS-dependent protein transport.

PubMed: 41266322
DOI: 10.1038/s41467-025-65003-8

実験手法

ELECTRON MICROSCOPY (3.7 Å)