{"title":"次生输运机制演化的结构窗口","authors":"Samuel P. Berry, Rachelle Gaudet","doi":"10.1038/s41594-025-01625-2","DOIUrl":null,"url":null,"abstract":"Protein sequence signatures suggest that eons ago, a bacterial glutamate transporter lost its sodium coupling to make way for a shift to proton coupling. A study now maps this ancient transition in biochemical and structural detail to better understand how secondary transporters control their energetics.","PeriodicalId":18822,"journal":{"name":"Nature structural & molecular biology","volume":"25 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-08-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"A structural window into the evolution of secondary transport mechanisms\",\"authors\":\"Samuel P. Berry, Rachelle Gaudet\",\"doi\":\"10.1038/s41594-025-01625-2\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Protein sequence signatures suggest that eons ago, a bacterial glutamate transporter lost its sodium coupling to make way for a shift to proton coupling. A study now maps this ancient transition in biochemical and structural detail to better understand how secondary transporters control their energetics.\",\"PeriodicalId\":18822,\"journal\":{\"name\":\"Nature structural & molecular biology\",\"volume\":\"25 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2025-08-25\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature structural & molecular biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1038/s41594-025-01625-2\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature structural & molecular biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1038/s41594-025-01625-2","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
A structural window into the evolution of secondary transport mechanisms
Protein sequence signatures suggest that eons ago, a bacterial glutamate transporter lost its sodium coupling to make way for a shift to proton coupling. A study now maps this ancient transition in biochemical and structural detail to better understand how secondary transporters control their energetics.