6S3W

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

Summary for 6S3W

• Entry DOI: 10.2210/pdb6s3w/pdb
• NMR Information: BMRB: 27397
• Descriptor: TolBp, Cell envelope integrity/translocation protein TolA (2 entities in total)
• Functional Keywords: tola, tolb, pal, bacterial outer membrane, protein binding
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 2
• Total formula weight: 15053.87

Authors

Kleanthous, C.,Redfield, C.,Rajasekar, K.,Holmes, P. (deposition date: 2019-06-26, release date: 2020-03-25, Last modification date: 2024-07-03)

Primary citation

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

Experimental method

SOLUTION NMR