{"title":"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","authors":"Ko On Lee, J. Suh","doi":"10.6564/JKMRS.2017.21.1.020","DOIUrl":null,"url":null,"abstract":"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.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"21 1","pages":"20-25"},"PeriodicalIF":0.4000,"publicationDate":"2017-03-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":"{\"title\":\"Backbone Assignment of Phosphorylated Cytoplasmic Domain B of Mannitol Transporter IIMtl in Thermoanaerobacter Tengcongensis\",\"authors\":\"Ko On Lee, J. Suh\",\"doi\":\"10.6564/JKMRS.2017.21.1.020\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"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.\",\"PeriodicalId\":17414,\"journal\":{\"name\":\"Journal of the Korean magnetic resonance society\",\"volume\":\"21 1\",\"pages\":\"20-25\"},\"PeriodicalIF\":0.4000,\"publicationDate\":\"2017-03-20\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"1\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of the Korean magnetic resonance society\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.6564/JKMRS.2017.21.1.020\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMICAL RESEARCH METHODS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of the Korean magnetic resonance society","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.6564/JKMRS.2017.21.1.020","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}
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.