4i3c: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4i3c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anguilla_japonica Anguilla japonica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I3C FirstGlance]. <br> | <table><tr><td colspan='2'>[[4i3c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anguilla_japonica Anguilla japonica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I3C FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLR:3-[5-[(Z)-(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-2-[[5-[(Z)-(3-ethenyl-4-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-3-(3-hydroxy-3-oxopropyl)-4-methyl-1H-pyrrol-2-yl]methyl]-4-methyl-1H-pyrrol-3-yl]propanoic+acid'>BLR</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.001Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLR:3-[5-[(Z)-(4-ethenyl-3-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-2-[[5-[(Z)-(3-ethenyl-4-methyl-5-oxidanylidene-pyrrol-2-ylidene)methyl]-3-(3-hydroxy-3-oxopropyl)-4-methyl-1H-pyrrol-2-yl]methyl]-4-methyl-1H-pyrrol-3-yl]propanoic+acid'>BLR</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=4i3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3c OCA], [https://pdbe.org/4i3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i3c RCSB], [https://www.ebi.ac.uk/pdbsum/4i3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i3c ProSAT]</span></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=4i3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3c OCA], [https://pdbe.org/4i3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i3c RCSB], [https://www.ebi.ac.uk/pdbsum/4i3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i3c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 17:12, 8 November 2023
Crystal structure of fluorescent protein UnaG N57Q mutantCrystal structure of fluorescent protein UnaG N57Q mutant
Structural highlights
FunctionUNAG_ANGJA Beta-barrel protein that binds unconjugated bilirubin with high affinity. Excitation of the bilirubin-bound protein gives rise to green fluorescence, both under normoxia and hypoxia. The apoprotein is not fluorescent. Does not emit fluorescence in the presence of ditauro-bilirubin, urobilin or biliverdin.[1] Publication Abstract from PubMedThe fluorescent protein toolbox has revolutionized experimental biology. Despite this advance, no fluorescent proteins have been identified from vertebrates, nor has chromogenic ligand-inducible activation or clinical utility been demonstrated. Here, we report the cloning and characterization of UnaG, a fluorescent protein from Japanese eel. UnaG belongs to the fatty-acid-binding protein (FABP) family, and expression in eel is restricted to small-diameter muscle fibers. On heterologous expression in cell lines or mouse brain, UnaG produces oxygen-independent green fluorescence. Remarkably, UnaG fluorescence is triggered by an endogenous ligand, bilirubin, a membrane-permeable heme metabolite and clinical health biomarker. The holoUnaG structure at 1.2 A revealed a biplanar coordination of bilirubin by reversible pi-conjugation, and we used this high-affinity and high-specificity interaction to establish a fluorescence-based human bilirubin assay with promising clinical utility. UnaG will be the prototype for a versatile class of ligand-activated fluorescent proteins, with applications in research, medicine, and bioengineering. A bilirubin-inducible fluorescent protein from eel muscle.,Kumagai A, Ando R, Miyatake H, Greimel P, Kobayashi T, Hirabayashi Y, Shimogori T, Miyawaki A Cell. 2013 Jun 20;153(7):1602-11. doi: 10.1016/j.cell.2013.05.038. Epub 2013 Jun , 13. PMID:23768684[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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