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多杀巴斯德氏菌毒素膜定位结构域的主链和侧链共振归属

Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurella multocida toxin.

作者信息

Brothers Michael C, Geissler Brett, Hisao Grant S, Satchell Karla J F, Wilson Brenda A, 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 Apr;8(1):221-4. doi: 10.1007/s12104-013-9487-1. 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 (MLD) from Pasteurella multocida toxin (PMT) in its solution state. We have assigned 99% of all backbone and side-chain carbon atoms, including 99% of all backbone residues excluding proline amide nitrogens. Secondary chemical shift analysis using TALOS+ demonstrates four helices, which align with those observed within the MLD in the crystal structure of the C-terminus of PMT (PDB 2EBF) and confirm the use of the available crystal structures as templates for the isolated MLDs.

摘要

给出了多杀巴斯德氏菌毒素(PMT)的分离四螺旋束膜定位结构域(MLD)在溶液状态下的氢(¹H)、碳(¹³C)和氮(¹⁵N)化学位移归属。我们已归属了所有主链和侧链碳原子的99%,包括除脯氨酸酰胺氮以外所有主链残基的99%。使用TALOS+进行的二级化学位移分析表明有四条螺旋,这与PMT C端晶体结构(PDB 2EBF)中MLD内观察到的螺旋一致,并证实可将现有的晶体结构用作分离MLD的模板。

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