NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa
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...
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| Format: | Article |
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PeerJ Inc.
2018-08-01
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| Series: | PeerJ |
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| Online Access: | https://peerj.com/articles/5412.pdf |
| _version_ | 1797417831406501888 |
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| author | Jesper S. Oeemig O.H. Samuli Ollila Hideo Iwaï |
| author_facet | Jesper S. Oeemig O.H. Samuli Ollila Hideo Iwaï |
| author_sort | Jesper S. Oeemig |
| collection | DOAJ |
| description | 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 Escherichia coli TonB have been previously reported. Here we determined the solution NMR structure of a 96-residue fragment of Pseudomonas aeruginosa TonB (PaTonB-96). The structure shows a monomeric structure with the flexible C-terminal region (residues 338–342), different from the NMR structure of E. coli TonB (EcTonB-137). The extended and flexible C-terminal residues are confirmed by 15N relaxation analysis and molecular dynamics simulation. We created models for the PaTonB-96/TonB box interaction and propose that the internal fluctuations of PaTonB-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. |
| first_indexed | 2024-03-09T06:24:19Z |
| format | Article |
| id | doaj.art-e5dae9de082f4964a4a56260696d4390 |
| institution | Directory Open Access Journal |
| issn | 2167-8359 |
| language | English |
| last_indexed | 2024-03-09T06:24:19Z |
| publishDate | 2018-08-01 |
| publisher | PeerJ Inc. |
| record_format | Article |
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| spelling | doaj.art-e5dae9de082f4964a4a56260696d43902023-12-03T11:30:04ZengPeerJ Inc.PeerJ2167-83592018-08-016e541210.7717/peerj.5412NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosaJesper S. Oeemig0O.H. Samuli Ollila1Hideo Iwaï2Research Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Helsinki, FinlandResearch Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Helsinki, FinlandResearch Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Helsinki, FinlandThe 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 Escherichia coli TonB have been previously reported. Here we determined the solution NMR structure of a 96-residue fragment of Pseudomonas aeruginosa TonB (PaTonB-96). The structure shows a monomeric structure with the flexible C-terminal region (residues 338–342), different from the NMR structure of E. coli TonB (EcTonB-137). The extended and flexible C-terminal residues are confirmed by 15N relaxation analysis and molecular dynamics simulation. We created models for the PaTonB-96/TonB box interaction and propose that the internal fluctuations of PaTonB-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.https://peerj.com/articles/5412.pdfTonBNMRNMR structure15N relaxationMolecular dynamicsBtuB |
| spellingShingle | Jesper S. Oeemig O.H. Samuli Ollila Hideo Iwaï NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa PeerJ TonB NMR NMR structure 15N relaxation Molecular dynamics BtuB |
| title | NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa |
| title_full | NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa |
| title_fullStr | NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa |
| title_full_unstemmed | NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa |
| title_short | NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa |
| title_sort | nmr structure of the c terminal domain of tonb protein from pseudomonas aeruginosa |
| topic | TonB NMR NMR structure 15N relaxation Molecular dynamics BtuB |
| url | https://peerj.com/articles/5412.pdf |
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