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镉核磁共振实验揭示了酵母剪接蛋白Bud31p溶液结构中一个异常的金属簇。

Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p.

作者信息

van Roon Anne-Marie M, Yang Ji-Chun, Mathieu Daniel, Bermel Wolfgang, Nagai Kiyoshi, Neuhaus David

机构信息

MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH (UK).

Bruker BioSpin GmbH, Silberstreifen, 76287 Rheinstetten (Germany).

出版信息

Angew Chem Weinheim Bergstr Ger. 2015 Apr 13;127(16):4943-4946. doi: 10.1002/ange.201412210. Epub 2015 Feb 20.

Abstract

Establishing the binding topology of structural zinc ions in proteins is an essential part of their structure determination by NMR spectroscopy. Using Cd NMR experiments with Cd-substituted samples is a useful approach but has previously been limited mainly to very small protein domains. Here we used Cd NMR spectroscopy during structure determination of Bud31p, a 157-residue yeast protein containing an unusual ZnCys cluster, demonstrating that recent hardware developments make this approach feasible for significantly larger systems.

摘要

确定蛋白质中结构锌离子的结合拓扑结构是通过核磁共振光谱法确定其结构的重要组成部分。使用镉取代样品进行镉核磁共振实验是一种有用的方法,但此前主要限于非常小的蛋白质结构域。在这里,我们在含有不寻常ZnCys簇的157个残基酵母蛋白Bud31p的结构测定过程中使用了镉核磁共振光谱法,证明最近的硬件发展使这种方法对于大得多的系统也可行。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3a8f/4954022/bde5c4a57278/ANGE-127-4943-g001.jpg

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