高温厌氧杆菌甘油醇转运蛋白IIMtl磷酸化细胞质结构域B的主链定位

IF 0.4 Q4 BIOCHEMICAL RESEARCH METHODS Journal of the Korean magnetic resonance society Pub Date : 2017-03-20 DOI:10.6564/JKMRS.2017.21.1.020
Ko On Lee, J. Suh
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引用次数: 1

摘要

甘露糖醇转运酶II-Mtl的细胞质结构域A和B在大肠杆菌中共价连接,但在滕康热厌氧菌中单独表达。结构域B(Tt-IIB-Mtl)的磷酸化显著增加了滕粥T.IIA-Mtl与结构域A的结合亲和力。为了理解蛋白质磷酸化增强结构域-结构域相互作用的结构基础,我们使用一套标准的三重共振实验获得了磷酸化-Tt-IIB-Mtl的NMR骨架分配。我们的结果将有助于监测磷酸化活性位点和结合界面的化学位移变化。
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Backbone Assignment of Phosphorylated Cytoplasmic Domain B of Mannitol Transporter IIMtl in Thermoanaerobacter Tengcongensis
The cytoplasmic domains A and B of the mannitol transporter enzyme II Mtl are covalently linked in Escherichia coli , but separately expressed in Thermoanaerobacter Tengcongensis . The phosphorylation of domain B ( Tt IIB Mtl ) substantially increases the binding affinity to the domain A ( Tt IIA Mtl ) in T. Tengcongensis . To understand the structural basis of the enhanced domain - domain interaction by protein phosphorylation, we obtained NMR backbone assignments of the phospho- Tt IIB Mtl using a standard suite of triple resonance experiments. Our results will be useful to monitor chemical shift changes at the active site of phosphorylation and the binding interfaces.
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Journal of the Korean magnetic resonance society
Journal of the Korean magnetic resonance society BIOCHEMICAL RESEARCH METHODS-
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