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

Biomol NMR Assign. 2014 Oct;8(2):225-8. doi: 10.1007/s12104-013-9488-0. Epub 2013 Jun 14.


(1)H, (13)C, and (15)N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain from the domain of unknown function 5 (DUF5) effector (MLD(VvDUF5)) 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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Toxins / chemistry*
  • Bacterial Toxins / metabolism*
  • Cell Membrane / metabolism*
  • Nuclear Magnetic Resonance, Biomolecular*
  • Protein Structure, Secondary
  • Protein Transport
  • Vibrio vulnificus*


  • Bacterial Toxins
  • RtxA protein, Vibrio cholerae