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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.

SUBMITTER: Brothers MC

PROVIDER: S-EPMC3859805 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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

Brothers Michael C MC Geissler Brett B Hisao Grant S GS Satchell Karla J F KJ Wilson Brenda A BA Rienstra Chad M CM

Biomolecular NMR assignments 20130614 1

(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-terminu ...[more]

PMID: 23765284

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