{"title":"Structural insights into retinal-free microbial rhodopsins","authors":"Zhenmei Xu, Yuanzheng He","doi":"10.1016/j.str.2025.08.005","DOIUrl":null,"url":null,"abstract":"Rhodopsins typically harness light energy through the covalently bound retinal cofactor. However, some rhodopsins have lost this ability during evolution. In this issue of <em>Structure</em>, Kovalev et al.<span><span><sup>1</sup></span></span> present the cryo-electron microscopy (cryo-EM) structure of a retinal-free flotillin-associated rhodopsin (FArhodopsin), providing new insights into their architecture and potential non-photochemical functions.","PeriodicalId":22168,"journal":{"name":"Structure","volume":"29 1","pages":""},"PeriodicalIF":4.3000,"publicationDate":"2025-09-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Structure","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1016/j.str.2025.08.005","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Rhodopsins typically harness light energy through the covalently bound retinal cofactor. However, some rhodopsins have lost this ability during evolution. In this issue of Structure, Kovalev et al.1 present the cryo-electron microscopy (cryo-EM) structure of a retinal-free flotillin-associated rhodopsin (FArhodopsin), providing new insights into their architecture and potential non-photochemical functions.
期刊介绍:
Structure aims to publish papers of exceptional interest in the field of structural biology. The journal strives to be essential reading for structural biologists, as well as biologists and biochemists that are interested in macromolecular structure and function. Structure strongly encourages the submission of manuscripts that present structural and molecular insights into biological function and mechanism. Other reports that address fundamental questions in structural biology, such as structure-based examinations of protein evolution, folding, and/or design, will also be considered. We will consider the application of any method, experimental or computational, at high or low resolution, to conduct structural investigations, as long as the method is appropriate for the biological, functional, and mechanistic question(s) being addressed. Likewise, reports describing single-molecule analysis of biological mechanisms are welcome.
In general, the editors encourage submission of experimental structural studies that are enriched by an analysis of structure-activity relationships and will not consider studies that solely report structural information unless the structure or analysis is of exceptional and broad interest. Studies reporting only homology models, de novo models, or molecular dynamics simulations are also discouraged unless the models are informed by or validated by novel experimental data; rationalization of a large body of existing experimental evidence and making testable predictions based on a model or simulation is often not considered sufficient.