Structural insights into retinal-free microbial rhodopsins

Zhenmei Xu; Yuanzheng He

doi:10.1016/j.str.2025.08.005

Structural insights into retinal-free microbial rhodopsins

Zhenmei Xu^*
, Yuanzheng He^*

^*Corresponding author for this work

Faculty of Life Sciences and Medicine

School of Life Science and Technology, Harbin Institute of Technology

Research output: Contribution to journal › Comment/debate

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.

Original language	English
Pages (from-to)	1457-1458
Number of pages	2
Journal	Structure
Volume	33
Issue number	9
DOIs	https://doi.org/10.1016/j.str.2025.08.005
State	Published - 4 Sep 2025

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10.1016/j.str.2025.08.005

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title = "Structural insights into retinal-free microbial rhodopsins",

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.",

author = "Zhenmei Xu and Yuanzheng He",

note = "Publisher Copyright: {\textcopyright} 2025 Elsevier Inc.",

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AU - Xu, Zhenmei

AU - He, Yuanzheng

PY - 2025/9/4

Y1 - 2025/9/4

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/105014358834

U2 - 10.1016/j.str.2025.08.005

DO - 10.1016/j.str.2025.08.005

M3 - 评论/辩论

C2 - 40912240

AN - SCOPUS:105014358834

SN - 0969-2126

VL - 33

SP - 1457

EP - 1458

JO - Structure

JF - Structure

IS - 9

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Structural insights into retinal-free microbial rhodopsins

Abstract

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