Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurella multocida toxin

Biomol NMR Assign. 2014 Apr;8(1):221-4. doi: 10.1007/s12104-013-9487-1. Epub 2013 Jun 14.

Abstract

(1)H, (13)C, and (15)N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain (MLD) from Pasteurella multocida toxin (PMT) in its solution state. We have assigned 99% of all backbone and side-chain carbon atoms, including 99% of all backbone residues excluding proline amide nitrogens. Secondary chemical shift analysis using TALOS+ demonstrates four helices, which align with those observed within the MLD in the crystal structure of the C-terminus of PMT (PDB 2EBF) and confirm the use of the available crystal structures as templates for the isolated MLDs.

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

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Toxins / chemistry*
  • Cell Membrane / chemistry*
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular*
  • Pasteurella multocida / metabolism*
  • Protein Structure, Tertiary

Substances

  • Bacterial Proteins
  • Bacterial Toxins
  • Pasteurella multocida toxin