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Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurella multocida toxin |
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| Authors: | Michael C Brothers Brett Geissler Grant S Hisao Karla J F Satchell Brenda A Wilson Chad M Rienstra |
| Institution: | 1. Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA 2. Department of Microbiology-Immunology, Northwestern University, Chicago, IL, 60611, USA 3. Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA 4. Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA 5. Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA |
| Abstract: | 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. |
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