4.0 Article

Backbone and side-chain assignments of an effector membrane localization domain from Vibrio vulnificus MARTX toxin

Journal

BIOMOLECULAR NMR ASSIGNMENTS
Volume 8, Issue 2, Pages 225-228

Publisher

SPRINGER
DOI: 10.1007/s12104-013-9488-0

Keywords

Membrane localization domain; Four helical bundle; MARTX toxins; Pasteurella multocida toxin

Funding

  1. NIH [AI051490, AI092825]
  2. Pathogenesis of Infectious Disease award from the Burroughs Wellcome Fund
  3. NIH/NIAID [AI038396]
  4. University of Illinois
  5. NIH/CBITG [T32 GM070421]
  6. Department of Homeland Security Fellowship

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H-1, C-13, and N-15 chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain from the domain of unknown function 5 (DUF5) effector (MLDVvDUF5) of the MARTX toxin from Vibrio vulnificus in its solution state. We have assigned 97 % of all backbone and side-chain carbon atoms, including 96 % of all backbone residues. Secondary chemical shift analysis using TALOS+ demonstrates four helices that align with those predicted by structure homology modeling using the MLDs of Pasteurella multocida toxin (PMT) and the clostridial TcdB and TcsL toxins as templates. Future studies will be towards solving the structure and determining the dynamics in the solution state.

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