9CCG

Fusobacterium nucleatum BamA-Fab 9 complex

9CCG の概要

• エントリーDOI: 10.2210/pdb9ccg/pdb
• EMDBエントリー: 45442
• 分子名称: POTRA domain-containing protein, Fab 9 heavy chain, Fab 9 light chain (3 entities in total)
• 機能のキーワード: proteomics, protein folding, membrane protein, structural biology
• 由来する生物種: Fusobacterium nucleatum; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 246716.12

構造登録者

Overly Cottom, C.,Noinaj, N. (登録日: 2024-06-21, 公開日: 2025-09-17, 最終更新日: 2025-11-19)

主引用文献

Cottom, C.O.,Heinz, E.,Erramilli, S.,Kossiakoff, A.,Slade, D.J.,Noinaj, N.
Characterization of the OMP biogenesis machinery in Fusobacterium nucleatum.
Structure, 33:1878-, 2025

PubMed Abstract: F. nucleatum is a Gram-negative bacteria that causes oral infections and is linked to colorectal cancer. Pathogenicity relies on a type of β-barrel outer membrane protein (OMP) called an autotransporter. The biogenesis of OMPs is typically mediated by the barrel assembly machinery (BAM) complex. In this study, we investigate the evolution, composition, and structure of the OMP biogenesis machinery in F. nucleatum. Our bioinformatics and proteomics analyses indicate that OMP biogenesis in F. nucleatum is mediated solely by the core component BamA. The structure of FnBamA highlights distinct features, including four POTRA domains and a C-terminal 16-stranded β-barrel domain observed as an inverted dimer. FnBamA represents the original composition of the assembly machinery, and a duplication event that resulted in BamA and TamA occurred after the split of other lineages, including the Proteobacteria, from the Fusobacteria. FnBamA, therefore, likely serves a singular role in the biogenesis of all OMPs.

PubMed: 40897170
DOI: 10.1016/j.str.2025.08.008

実験手法

ELECTRON MICROSCOPY (3.87 Å)