6S3W

Solution NMR Structure of TolAIII Bound to a Peptide Derived from the N-terminus of TolB

6S3W の概要

• エントリーDOI: 10.2210/pdb6s3w/pdb
• NMR情報: BMRB: 27397
• 分子名称: TolBp, Cell envelope integrity/translocation protein TolA (2 entities in total)
• 機能のキーワード: tola, tolb, pal, bacterial outer membrane, protein binding
• 由来する生物種: Pseudomonas aeruginosa; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15053.87

構造登録者

Kleanthous, C.,Redfield, C.,Rajasekar, K.,Holmes, P. (登録日: 2019-06-26, 公開日: 2020-03-25, 最終更新日: 2024-07-03)

主引用文献

Szczepaniak, J.,Holmes, P.,Rajasekar, K.,Kaminska, R.,Samsudin, F.,Inns, P.G.,Rassam, P.,Khalid, S.,Murray, S.M.,Redfield, C.,Kleanthous, C.
The lipoprotein Pal stabilises the bacterial outer membrane during constriction by a mobilisation-and-capture mechanism.
Nat Commun, 11:1305-1305, 2020

PubMed Abstract: Coordination of outer membrane constriction with septation is critical to faithful division in Gram-negative bacteria and vital to the barrier function of the membrane. This coordination requires the recruitment of the peptidoglycan-binding outer-membrane lipoprotein Pal at division sites by the Tol system. Here, we show that Pal accumulation at Escherichia coli division sites is a consequence of three key functions of the Tol system. First, Tol mobilises Pal molecules in dividing cells, which otherwise diffuse very slowly due to their binding of the cell wall. Second, Tol actively captures mobilised Pal molecules and deposits them at the division septum. Third, the active capture mechanism is analogous to that used by the inner membrane protein TonB to dislodge the plug domains of outer membrane TonB-dependent nutrient transporters. We conclude that outer membrane constriction is coordinated with cell division by active mobilisation-and-capture of Pal at division septa by the Tol system.

PubMed: 32161270
DOI: 10.1038/s41467-020-15083-5

実験手法

SOLUTION NMR