6FIP

Solution NMR structure of Pseudomonas aeruginosa TonB CTD

Summary for 6FIP

• Entry DOI: 10.2210/pdb6fip/pdb
• NMR Information: BMRB: 34235
• Descriptor: Protein TonB (1 entity in total)
• Functional Keywords: tonb, tonb box, gram-negative bacteria, transport protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 11503.45

Authors

Oeemig, J.S.,Samuli Ollila, O.H.,Heikkinen, H.A.,Iwai, H. (deposition date: 2018-01-19, release date: 2018-08-29, Last modification date: 2024-06-19)

Primary citation

Oeemig, J.S.,Ollila, O.H.S.,Iwai, H.
NMR structure of the C-terminal domain of TonB protein fromPseudomonas aeruginosa.
PeerJ, 6:e5412-e5412, 2018

PubMed Abstract: The TonB protein plays an essential role in the energy transduction system to drive active transport across the outer membrane (OM) using the proton-motive force of the cytoplasmic membrane of Gram-negative bacteria. The C-terminal domain (CTD) of TonB protein is known to interact with the conserved TonB box motif of TonB-dependent OM transporters, which likely induces structural changes in the OM transporters. Several distinct conformations of differently dissected CTDs of TonB have been previously reported. Here we determined the solution NMR structure of a 96-residue fragment of TonB (TonB-96). The structure shows a monomeric structure with the flexible C-terminal region (residues 338-342), different from the NMR structure of TonB (TonB-137). The extended and flexible C-terminal residues are confirmed by N relaxation analysis and molecular dynamics simulation. We created models for the TonB-96/TonB box interaction and propose that the internal fluctuations of TonB-96 makes it more accessible for the interactions with the TonB box and possibly plays a role in disrupting the plug domain of the TonB-dependent OM transporters.

PubMed: 30186676
DOI: 10.7717/peerj.5412

Experimental method

SOLUTION NMR