4i3b: Difference between revisions
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==Crystal structure of fluorescent protein UnaG wild type== | ==Crystal structure of fluorescent protein UnaG wild type== | ||
<StructureSection load='4i3b' size='340' side='right' caption='[[4i3b]], [[Resolution|resolution]] 1.20Å' scene=''> | <StructureSection load='4i3b' size='340' side='right' caption='[[4i3b]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i3c|4i3c]], [[4i3d|4i3d]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i3c|4i3c]], [[4i3d|4i3d]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4i3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i3b RCSB], [http://www.ebi.ac.uk/pdbsum/4i3b PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4i3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3b OCA], [http://pdbe.org/4i3b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i3b RCSB], [http://www.ebi.ac.uk/pdbsum/4i3b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i3b ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4i3b" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:25, 23 December 2016
Crystal structure of fluorescent protein UnaG wild typeCrystal structure of fluorescent protein UnaG wild type
Structural highlights
Function[UNAG_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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