The membrane localization domains of two distinct bacterial toxins form a 4‐helix‐bundle in solution |
| |
Authors: | Grant S. Hisao Michael C. Brothers Mengfei Ho Brenda A. Wilson Chad M. Rienstra |
| |
Affiliation: | 1. Department of Chemistry, University of Illinois at Urbana‐Champaign, Illinois;2. Department of Microbiology, University of Illinois at Urbana‐Champaign, Illinois;3. Department of Biochemistry, University of Illinois at Urbana‐Champaign, Illinois;4. Center for Biophysics and Quantitative Biology, University of Illinois at Urbana‐Champaign, Illinois |
| |
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. |
| |
Keywords: | Pasteurella multocida Vibrio vulnificus bacterial toxin membrane localization domains solution NMR spectroscopy 4‐helix‐bundle |
|
|