Backbone and side-chain assignments of an effector membrane localization domain from Vibrio vulnificus MARTX toxin

被引：3
|
作者：
Brothers, Michael C. [1 ]
Geissler, Brett [2 ]
Hisao, Grant S. [1 ]
Wilson, Brenda A. [3 ]
Satchell, Karla J. F. [2 ]
Rienstra, Chad M. [1 ,4 ,5 ]
机构：
[1] Univ Illinois, Dept Chem, Urbana, IL 61801 USA
[2] Northwestern Univ, Dept Microbiol Immunol, Chicago, IL 60611 USA
[3] Univ Illinois, Dept Microbiol, Urbana, IL 61801 USA
[4] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA
[5] Univ Illinois, Ctr Biophys & Computat Biol, Urbana, IL 61801 USA
来源：
BIOMOLECULAR NMR ASSIGNMENTS | 2014年 / 8卷 / 02期
关键词：
Membrane localization domain; Four helical bundle; MARTX toxins; Pasteurella multocida toxin; LARGER PROTEINS; SPECTROSCOPY; RESONANCES; SPECTRA; AMIDE;
D O I：
10.1007/s12104-013-9488-0
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
H-1, C-13, and N-15 chemical shift assignments are presented for the isolated four-helical bundle membrane localization domain from the domain of unknown function 5 (DUF5) effector (MLDVvDUF5) 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.
引用
收藏
页码：225 / 228
页数：4
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