+検索条件
-Structure paper
| タイトル | A shared mechanism for Bacteroidota protein transport and gliding motility. |
|---|---|
| ジャーナル・号・ページ | Nat Commun, Vol. 16, Issue 1, Page 10217, Year 2025 |
| 掲載日 | 2025年11月20日 |
著者 | Xiaolong Liu / Marieta Avramova / Justin C Deme / Rachel L Jones / Camilla A K Lundgren / Susan M Lea / Ben C Berks / ![]() |
| PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:41266322 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.7 - 3.7 Å |
| 構造データ | EMDB-48835, PDB-9n2d: EMDB-48836, PDB-9n2e: |
| 化合物 | ![]() ChemComp-DGA: ![]() ChemComp-JSG: ![]() ChemComp-PTY: ![]() ChemComp-MAN: ![]() ChemComp-PLM: ![]() ChemComp-CA: ![]() ChemComp-HOH: |
| 由来 |
|
キーワード | MEMBRANE PROTEIN / BAM complex / BamA / BamD / BamG / BamH / BamM / BamP / outer-membrane proteins / OMP / BamAP complex |
ムービー
コントローラー
構造ビューア
万見文献について



著者

リンク










flavobacterium johnsoniae uw101 (バクテリア)
キーワード