NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F18%3A00493387" target="_blank" >RIV/61388963:_____/18:00493387 - isvavai.cz</a>

Result on the web

<a href="https://peerj.com/articles/5412/" target="_blank" >https://peerj.com/articles/5412/</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.7717/peerj.5412" target="_blank" >10.7717/peerj.5412</a>

Result language

angličtina

Original language name

NMR structure of the C-terminal domain of TonB protein from Pseudomonas aeruginosa

Original language 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 N-15 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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

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Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2018

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

PeerJ

ISSN

2167-8359

e-ISSN

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Volume of the periodical

6

Issue of the periodical within the volume

Aug 27

Country of publishing house

US - UNITED STATES

Number of pages

19

Pages from-to

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UT code for WoS article

000443310500002

EID of the result in the Scopus database

2-s2.0-85052490979