6FIP

Solution NMR structure of Pseudomonas aeruginosa TonB CTD

6FIP の概要

• エントリーDOI: 10.2210/pdb6fip/pdb
• NMR情報: BMRB: 34235
• 分子名称: Protein TonB (1 entity in total)
• 機能のキーワード: tonb, tonb box, gram-negative bacteria, transport protein
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11503.45

構造登録者

Oeemig, J.S.,Samuli Ollila, O.H.,Heikkinen, H.A.,Iwai, H. (登録日: 2018-01-19, 公開日: 2018-08-29, 最終更新日: 2024-06-19)

主引用文献

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

実験手法

SOLUTION NMR