The membrane localization domains of two distinct bacterial toxins form a 4‐helix‐bundle in solution. (14th February 2017)

• Record Type: Journal Article
• Authors: Hisao, Grant S.; Brothers, Michael C.; Ho, Mengfei; Wilson, Brenda A.; Rienstra, Chad M.
• Is Part Of: Protein science. Volume 26:Number 3(2017)
• Page Start: 497
• Page End: 504
• Publication Date: 2017-02-14
• Subjects: Pasteurella multocida -- Vibrio vulnificus -- bacterial toxin -- membrane localization domains -- solution NMR spectroscopy -- 4‐helix‐bundle; Proteins -- Periodicals; 572.6
• DOI: 10.1002/pro.3097
• Languages: English
• ISSNs: 0961-8368

Abstract

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. Abstract : PDB Code(s):2N9V ;2N9W