Immunity protein release from a cell-bound nuclease colicin complex requires global conformational rearrangement
Author:
Affiliation:
1. School of Life Sciences; Centre for Biomolecular Sciences; University of Nottingham; University Park; Nottingham; NG7 2RD; United Kingdom
2. Department of Biochemistry; University of Oxford; South Parks Road; Oxford; OX1 3QU; United Kingdom
Publisher
Wiley
Subject
Microbiology
Reference33 articles.
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2. Colicin biology;Cascales;Microbiol. Mol. Biol. Rev.,2007
3. Structural dynamics of the membrane translocation domain of colicin E9 and its interaction with TolB;Collins;J. Mol. Biol.,2002
4. Colicin E2 is still in contact with its receptor and import machinery when its nuclease domain enters the cytoplasm;Duché;J. Bacteriol.,2007
5. A force-activated trip switch triggers rapid dissociation of a colicin from its immunity protein;Farrance;PLoS Biol.,2013
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1. Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF;The EMBO Journal;2021-09-13
2. Transmembrane Epitope Delivery by Passive Protein Threading through the Pores of the OmpF Porin Trimer;Journal of the American Chemical Society;2020-07-02
3. Tools and Approaches for Dissecting Protein Bacteriocin Import in Gram-Negative Bacteria;Frontiers in Microbiology;2019-03-28
4. Lipopolysaccharides promote binding and unfolding of the antibacterial colicin E3 rRNAse domain;Biochimica et Biophysica Acta (BBA) - Biomembranes;2017-12
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