{"title":"鼠伤寒沙门菌质周葡萄糖/半乳糖受体的结构。","authors":"S. L. Mowbray, R. D. Smith, L. Cole","doi":"10.2210/PDB3GBP/PDB","DOIUrl":null,"url":null,"abstract":"The X-ray structure of the periplasmic glucose/galactose receptor (binding protein) of Salmonella typhimurium has been solved by the method of multiple isomorphous replacement and refined to a resolution of 2.4 A with an R-factor of 15.8%. The protein consists of two highly-similar structural domains with a bound sugar molecule trapped between. A combined sequence/structural approach is used to compare the structure of this protein to a similar arabinose receptor. The new sequence alignment obtained is used to analyze a number of features conserved for structural and functional reasons. This information allowed the prediction of similar features within the sequence of the analogous ribose receptor. Some of the consequences of the structures for chemotaxis and transport are discussed.","PeriodicalId":21112,"journal":{"name":"Receptor","volume":"PC-18 1","pages":"41-53"},"PeriodicalIF":0.0000,"publicationDate":"1991-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"27","resultStr":"{\"title\":\"Structure of the periplasmic glucose/galactose receptor of Salmonella typhimurium.\",\"authors\":\"S. L. Mowbray, R. D. Smith, L. Cole\",\"doi\":\"10.2210/PDB3GBP/PDB\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The X-ray structure of the periplasmic glucose/galactose receptor (binding protein) of Salmonella typhimurium has been solved by the method of multiple isomorphous replacement and refined to a resolution of 2.4 A with an R-factor of 15.8%. The protein consists of two highly-similar structural domains with a bound sugar molecule trapped between. A combined sequence/structural approach is used to compare the structure of this protein to a similar arabinose receptor. The new sequence alignment obtained is used to analyze a number of features conserved for structural and functional reasons. This information allowed the prediction of similar features within the sequence of the analogous ribose receptor. Some of the consequences of the structures for chemotaxis and transport are discussed.\",\"PeriodicalId\":21112,\"journal\":{\"name\":\"Receptor\",\"volume\":\"PC-18 1\",\"pages\":\"41-53\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1991-07-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"27\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Receptor\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.2210/PDB3GBP/PDB\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Receptor","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2210/PDB3GBP/PDB","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 27
摘要
鼠伤寒沙门菌质周葡萄糖/半乳糖受体(结合蛋白)的x射线结构采用多重同构置换法求解,得到分辨率为2.4 a, r因子为15.8%的结果。这种蛋白质由两个高度相似的结构域组成,中间夹着一个结合的糖分子。组合序列/结构方法用于比较该蛋白的结构与类似的阿拉伯糖受体。获得的新序列比对用于分析由于结构和功能原因而保守的许多特征。这一信息使得预测类似核糖受体序列中的相似特征成为可能。讨论了这些结构对趋化性和运输的影响。
Structure of the periplasmic glucose/galactose receptor of Salmonella typhimurium.
The X-ray structure of the periplasmic glucose/galactose receptor (binding protein) of Salmonella typhimurium has been solved by the method of multiple isomorphous replacement and refined to a resolution of 2.4 A with an R-factor of 15.8%. The protein consists of two highly-similar structural domains with a bound sugar molecule trapped between. A combined sequence/structural approach is used to compare the structure of this protein to a similar arabinose receptor. The new sequence alignment obtained is used to analyze a number of features conserved for structural and functional reasons. This information allowed the prediction of similar features within the sequence of the analogous ribose receptor. Some of the consequences of the structures for chemotaxis and transport are discussed.