Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurellamultocida toxin View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2013-06-14

AUTHORS

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

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. More... »

PAGES

221-224

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12104-013-9487-1

DOI

http://dx.doi.org/10.1007/s12104-013-9487-1

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1020699685

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23765284


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