Backbone assignment of CcdBG100T toxin from E.coli in complex with the toxin binding C-terminal domain of its cognate antitoxin CcdA

Nanda, B and Bhowmick, J and Varadarajan, R and Sarma, SP (2024) Backbone assignment of CcdBG100T toxin from E.coli in complex with the toxin binding C-terminal domain of its cognate antitoxin CcdA. In: Biomolecular NMR Assignments .

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Abstract

The CcdAB system expressed in the E.coli cells is a prototypical example of the bacterial toxin-antitoxin (TA) systems that ensure the survival of the bacterial population under adverse environmental conditions. The solution and crystal structures of CcdA, CcdB and of CcdB in complex with the toxin-binding C-terminal domain of CcdA have been reported. Our interest lies in the dynamics of CcdB-CcdA complex formation. Solution NMR studies have shown that CcdBG100T, in presence of saturating concentrations of CcdA-c, a truncated C-terminal fragment of CcdA exists in equilibrium between two major populations. Sequence specific backbone resonance assignments of both equilibrium forms of the ~ 27 kDa complex, have been obtained from a suite of triple resonance NMR experiments acquired on 2H, 13C, 15N enriched samples of CcdBG100T. Analysis of 1H, 13Cα, 13Cβ secondary chemical shifts, shows that both equilibrium forms of CcdBG100T have five beta-strands and one alpha-helix as the major secondary structural elements in the tertiary structure. The results of these studies are presented below. © The Author(s), under exclusive licence to Springer Nature B.V. 2024.

Item Type:	Journal Article
Publication:	Biomolecular NMR Assignments
Publisher:	Springer Science and Business Media B.V.
Additional Information:	The copyright for this article belongs to the publisher.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	18 Oct 2024 04:33
Last Modified:	18 Oct 2024 04:33
URI:	http://eprints.iisc.ac.in/id/eprint/86364

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