创伤弧菌MARTX毒素效应器膜定位结构域的主链和侧链归属
Backbone and side-chain assignments of an effector membrane localization domain from Vibrio vulnificus MARTX toxin.
作者信息
Brothers Michael C, Geissler Brett, Hisao Grant S, Wilson Brenda A, Satchell Karla J F, Rienstra Chad M
机构信息
Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL, 61801, USA.
出版信息
Biomol NMR Assign. 2014 Oct;8(2):225-8. doi: 10.1007/s12104-013-9488-0. Epub 2013 Jun 14.
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.
摘要
本文给出了创伤弧菌MARTX毒素中功能未知结构域5（DUF5）效应蛋白（MLD(VvDUF5)）分离出的四螺旋束膜定位结构域在溶液状态下的氢（¹H）、碳（¹³C）和氮（¹⁵N）化学位移归属。我们已对所有主链和侧链碳原子的97%进行了归属，包括所有主链残基的96%。使用TALOS+进行的二级化学位移分析表明，有四个螺旋与以多杀巴斯德氏菌毒素（PMT）以及梭菌属TcdB和TcsL毒素的MLD为模板通过结构同源性建模预测的螺旋一致。未来的研究将致力于解析该结构并确定其在溶液状态下的动力学。
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