title: Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurella multocida toxin.
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.
authors.affiliation: Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA.
authors.forename: Michael C
authors.initials: MC
authors.lastname: Brothers
authors.forename: Brett
authors.initials: B
authors.lastname: Geissler
authors.forename: Grant S
authors.initials: GS
authors.lastname: Hisao
authors.forename: Karla J F
authors.initials: KJ
authors.lastname: Satchell
authors.forename: Brenda A
authors.initials: BA
authors.lastname: Wilson
authors.forename: Chad M
authors.initials: CM
authors.lastname: Rienstra
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001427:Bacterial Toxins / Q000737:chemistry*; D002462:Cell Membrane / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D016979:Pasteurella multocida / Q000378:metabolism*; D017434:Protein Structure, Tertiary
chemical_list: D001426:Bacterial Proteins; D001427:Bacterial Toxins; C062258:Pasteurella multocida toxin