4i3c: Difference between revisions

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==Crystal structure of fluorescent protein UnaG N57Q mutant==
==Crystal structure of fluorescent protein UnaG N57Q mutant==
<StructureSection load='4i3c' size='340' side='right' caption='[[4i3c]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4i3c' size='340' side='right' caption='[[4i3c]], [[Resolution|resolution]] 2.00&Aring;' 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></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></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i3b|4i3b]], [[4i3d|4i3d]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4i3b|4i3b]], [[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=4i3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4i3c RCSB], [http://www.ebi.ac.uk/pdbsum/4i3c 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=4i3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3c OCA], [http://pdbe.org/4i3c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4i3c RCSB], [http://www.ebi.ac.uk/pdbsum/4i3c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4i3c ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4i3c" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 10:29, 23 December 2016

Crystal structure of fluorescent protein UnaG N57Q mutantCrystal structure of fluorescent protein UnaG N57Q mutant

Structural highlights

4i3c is a 2 chain structure with sequence from Angja. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

The 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

  1. Kumagai A, Ando R, Miyatake H, Greimel P, Kobayashi T, Hirabayashi Y, Shimogori T, Miyawaki A. A bilirubin-inducible fluorescent protein from eel muscle. Cell. 2013 Jun 20;153(7):1602-11. doi: 10.1016/j.cell.2013.05.038. Epub 2013 Jun , 13. PMID:23768684 doi:10.1016/j.cell.2013.05.038
  2. Kumagai A, Ando R, Miyatake H, Greimel P, Kobayashi T, Hirabayashi Y, Shimogori T, Miyawaki A. A bilirubin-inducible fluorescent protein from eel muscle. Cell. 2013 Jun 20;153(7):1602-11. doi: 10.1016/j.cell.2013.05.038. Epub 2013 Jun , 13. PMID:23768684 doi:10.1016/j.cell.2013.05.038

4i3c, resolution 2.00Å

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