View source for 9ebw


==Chimeric fluorescence biosensor formed from a lactate-binding protein and GFP, bound to lactate==
<StructureSection load='9ebw' size='340' side='right'caption='[[9ebw]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ebw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9EBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9EBW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.78&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LAC:LACTIC+ACID'>LAC</scene>, <scene name='pdbligand=SWG:2-[(4Z)-2-[(1R)-1-AMINO-2-HYDROXY-ETHYL]-4-(1H-INDOL-3-YLMETHYLIDENE)-5-OXO-IMIDAZOL-1-YL]ETHANOIC+ACID'>SWG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9ebw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ebw OCA], [https://pdbe.org/9ebw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ebw RCSB], [https://www.ebi.ac.uk/pdbsum/9ebw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ebw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O24911_HELPY O24911_HELPY] [https://www.uniprot.org/uniprot/GFP_AEQVI 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.
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== 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<ref>PMID:40048274</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 9ebw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aequorea victoria]]
[[Category: Helicobacter pylori 26695]]
[[Category: Large Structures]]
[[Category: Ambarian JA]]
[[Category: Davis KM]]
[[Category: Horwitz SM]]
[[Category: Jones R]]
[[Category: Waidmann L]]