Disulphide trapping of an in vivo energy-dependent conformation of Escherichia coli TonB protein
Author:
Publisher
Wiley
Subject
Molecular Biology,Microbiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2958.2004.04384.x/fullpdf
Reference40 articles.
1. Functional analysis of a C-terminally altered TonB protein of Escherichia coli;Anton;Gene,1991
2. The structurally related exbB and tolQ genes are interchangeable in conferring tonB-dependent colicin, bacteriophage, and albomycin sensitivity;Braun;J Bacteriol,1989
3. Aromatic-aromatic interaction: a mechanism of protein structure stabilization;Burley;Science,1985
4. Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter;Cadieux;Proc Natl Acad Sci USA,1999
5. Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold;Chang;J Biol Chem,2001
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1. In vivotests of theE. coliTonB system working model—interaction of ExbB with unknown proteins, identification of TonB-ExbD transmembrane heterodimers and PMF-dependent ExbD structures;2024-07-10
2. Studies on the Escherichia coli ExbD Transmembrane Domain, Residue L132, and an Inhibitory Cyclic Peptide;2022-09-26
3. The Ton Motor;Frontiers in Microbiology;2022-04-07
4. Identification of New In Vivo TonB-FepA Rendezvous Sites;2021-12-08
5. Structure and Stoichiometry of the Ton Molecular Motor;International Journal of Molecular Sciences;2020-01-07
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