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

Romain NavarroOlivier BornetLaetitia HouotRoland LloubesFrançoise GuerlesquinMatthieu Nouailler
Published in: Biomolecular NMR assignments (2016)
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, CTXΦ, that carries the cholera toxin encoding genes. A crucial step during phage infection requires a direct interaction between the CTXΦ 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).
Keyphrases
  • protein protein
  • amino acid
  • escherichia coli
  • endothelial cells
  • klebsiella pneumoniae
  • magnetic resonance
  • genome wide
  • multidrug resistant
  • transcription factor