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

Michael C. Brothers, Brett Geissler, Grant S. Hisao, Karla J.F. Satchell, Brenda A. Wilson, Chad M. Rienstra*

*Corresponding author for this work

Research output: Contribution to journalArticle

3 Scopus citations


1H, 13C, and 15N 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.

Original languageEnglish (US)
Pages (from-to)221-224
Number of pages4
JournalBiomolecular NMR Assignments
Issue number1
StatePublished - Apr 2014



  • C1 domain
  • Four helical bundle
  • Membrane localization domain
  • Pasteurella multocida toxin

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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