title: Backbone and side-chain assignments of an effector membrane localization domain from Vibrio vulnificus MARTX toxin.
abstract: (1)H, (13)C, and (15)N chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain from the domain of unknown function 5 (DUF5) effector (MLD(VvDUF5)) of the MARTX toxin from Vibrio vulnificus in its solution state. We have assigned 97% of all backbone and side-chain carbon atoms, including 96% of all backbone residues. Secondary chemical shift analysis using TALOS+ demonstrates four helices that align with those predicted by structure homology modeling using the MLDs of Pasteurella multocida toxin (PMT) and the clostridial TcdB and TcsL toxins as templates. Future studies will be towards solving the structure and determining the dynamics in the solution state.
authors.affiliation: Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA.
authors.forename: Michael C
authors.initials: MC
authors.lastname: Brothers
authors.forename: Brett
authors.initials: B
authors.lastname: Geissler
authors.forename: Grant S
authors.initials: GS
authors.lastname: Hisao
authors.forename: Brenda A
authors.initials: BA
authors.lastname: Wilson
authors.forename: Karla J F
authors.initials: KJ
authors.lastname: Satchell
authors.forename: Chad M
authors.initials: CM
authors.lastname: Rienstra
mesh_terms: D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D021381:Protein Transport; D041261:Vibrio vulnificus
chemical_list: D001427:Bacterial Toxins; C434464:RtxA protein, Vibrio cholerae