Structural highlights
Function
O24911_HELPY GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
Publication Abstract from PubMed
Genetically encoded biosensors can measure biochemical properties such as small-molecule concentrations with single-cell resolution, even in vivo. Despite their utility, these sensors are "black boxes": Very little is known about the structures of their low- and high-fluorescence states or what features are required to transition between them. We used LiLac, a lactate biosensor with a quantitative fluorescence-lifetime readout, as a model system to address these questions. X-ray crystal structures and engineered high-affinity metal bridges demonstrate that LiLac exhibits a large interdomain twist motion that pulls the fluorescent protein away from a "sealed," high-lifetime state in the absence of lactate to a "cracked," low-lifetime state in its presence. Understanding the structures and dynamics of LiLac will help to think about and engineer other fluorescent biosensors.
State-dependent motion of a genetically encoded fluorescent biosensor.,Rosen PC, Horwitz SM, Brooks DJ, Kim E, Ambarian JA, Waidmann L, Davis KM, Yellen G Proc Natl Acad Sci U S A. 2025 Mar 11;122(10):e2426324122. doi: , 10.1073/pnas.2426324122. Epub 2025 Mar 6. PMID:40048274[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rosen PC, Horwitz SM, Brooks DJ, Kim E, Ambarian JA, Waidmann L, Davis KM, Yellen G. State-dependent motion of a genetically encoded fluorescent biosensor. Proc Natl Acad Sci U S A. 2025 Mar 11;122(10):e2426324122. PMID:40048274 doi:10.1073/pnas.2426324122
