(1)H, (15)N and (13)C resonance assignments of the C-terminal domain of Vibrio cholerae TolA protein. - Archive ouverte HAL Access content directly
Journal Articles Biomol NMR Assign Year : 2016

(1)H, (15)N and (13)C resonance assignments of the C-terminal domain of Vibrio cholerae TolA protein.

Abstract

Vibrio cholerae is the bacterial causative agent of the human disease cholera. Non-pathogenic bacterium can be converted to pathogenic following infection by a filamentous phage, CTX?, that carries the cholera toxin encoding genes. A crucial step during phage infection requires a direct interaction between the CTX? minor coat protein (pIII(CTX)) and the C-terminal domain of V. cholerae TolA protein (TolAIIIvc). In order to get a better understanding of TolA function during the infection process, we have initiated a study of the V. cholerae TolAIII domain by 2D and 3D heteronuclear NMR. With the exception of the His-tag (H123-H128), 97 % of backbone (1)H, (15)N and (13)C resonances were assigned and the side chain assignments for 92 % of the protein were obtained (BMRB deposit with accession number 25689).
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Dates and versions

hal-01458180 , version 1 (06-02-2017)

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Romain Navarro, Olivier Bornet, Laetitia Houot, Roland Lloubes, Francoise Guerlesquin, et al.. (1)H, (15)N and (13)C resonance assignments of the C-terminal domain of Vibrio cholerae TolA protein.. Biomol NMR Assign, 2016, ⟨10.1007/s12104-016-9690-y⟩. ⟨hal-01458180⟩
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