Literature DB >> 27977897

The membrane localization domains of two distinct bacterial toxins form a 4-helix-bundle in solution.

Grant S Hisao1, Michael C Brothers1, Mengfei Ho2, Brenda A Wilson2, Chad M Rienstra1,3,4.   

Abstract

Membrane localization domain (MLD) was first proposed for a 4-helix-bundle motif in the crystal structure of the C1 domain of Pasteurella multocida toxin (PMT). This structure motif is also found in the crystal structures of several clostridial glycosylating toxins (TcdA, TcdB, TcsL, and TcnA). The Ras/Rap1-specific endopeptidase (RRSP) module of the multifunctional autoprocessing repeats-in-toxins (MARTX) toxin produced by Vibrio vulnificus has sequence homology to the C1-C2 domains of PMT, including a putative MLD. We have determined the solution structure for the MLDs in PMT and in RRSP using solution state NMR. We conclude that the MLDs in these two toxins assume a 4-helix-bundle structure in solution.
© 2016 The Protein Society.

Entities:  

Keywords:  4-helix-bundle; Pasteurella multocida; Vibrio vulnificus; bacterial toxin; membrane localization domains; solution NMR spectroscopy

Mesh:

Substances:

Year:  2017        PMID: 27977897      PMCID: PMC5326565          DOI: 10.1002/pro.3097

Source DB:  PubMed          Journal:  Protein Sci        ISSN: 0961-8368            Impact factor:   6.725


  26 in total

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

Authors:  Michael C Brothers; Brett Geissler; Grant S Hisao; Karla J F Satchell; Brenda A Wilson; Chad M Rienstra
Journal:  Biomol NMR Assign       Date:  2013-06-14       Impact factor: 0.731

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