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

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

Author information

1
Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA.

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.

PMID:
23765284
PMCID:
PMC3859805
DOI:
10.1007/s12104-013-9487-1
[Indexed for MEDLINE]
Free PMC Article

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