7rbw: Difference between revisions
New page: '''Unreleased structure''' The entry 7rbw is ON HOLD until Paper Publication Authors: Fedorov, E., Manoilov, K.Y., Verkhusha, V., Almo, S.C., Ghosh, A. Description: Structure of Bilive... |
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==Structure of Biliverdin-binding Serpin of Boana punctata (polka-dot tree frog)== | |||
<StructureSection load='7rbw' size='340' side='right'caption='[[7rbw]], [[Resolution|resolution]] 2.05Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7rbw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Boana_punctata Boana punctata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RBW 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]] 2.05Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</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=7rbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rbw OCA], [https://pdbe.org/7rbw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rbw RCSB], [https://www.ebi.ac.uk/pdbsum/7rbw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rbw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A7D7FB99_BOAPU A0A7D7FB99_BOAPU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Biliverdin-binding serpins (BBSs) are proteins that are responsible for coloration in amphibians and fluoresce in the near-infrared (NIR) spectral region. Here we produced the first functional recombinant BBS of the polka-dot treefrog Boana punctata (BpBBS), assembled with its biliverdin (BV) chromophore, and report its biochemical and photochemical characterization. We determined the crystal structure of BpBBS at 2.05 A resolution, which demonstrated its structural homology to the mammalian protease inhibitor alpha-1-antitrypsin. BV interaction with BpBBS was studied and it was found that the N-terminal polypeptide (residues 19-50) plays a critical role in the BV binding. By comparing BpBBS with the available NIR fluorescent proteins and expressing it in mammalian cells, we demonstrated its potential as a NIR imaging probe. These results provide insight into the non-inhibitory function of serpins, provide a basis for improving their performance in mammalian cells, and suggest possible paths for the development of BBS-based fluorescent probes. | |||
Structural and Functional Characterization of a Biliverdin-Binding Near-Infrared Fluorescent Protein From the Serpin Superfamily.,Manoilov KY, Ghosh A, Almo SC, Verkhusha VV J Mol Biol. 2021 Nov 16;434(2):167359. doi: 10.1016/j.jmb.2021.167359. PMID:34798132<ref>PMID:34798132</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Almo | <div class="pdbe-citations 7rbw" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Ghosh | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Boana punctata]] | |||
[[Category: Large Structures]] | |||
[[Category: Almo SC]] | |||
[[Category: Fedorov E]] | |||
[[Category: Ghosh A]] | |||
[[Category: Manoilov KY]] | |||
[[Category: Verkhusha V]] | |||
Latest revision as of 19:28, 18 October 2023
Structure of Biliverdin-binding Serpin of Boana punctata (polka-dot tree frog)Structure of Biliverdin-binding Serpin of Boana punctata (polka-dot tree frog)
Structural highlights
FunctionPublication Abstract from PubMedBiliverdin-binding serpins (BBSs) are proteins that are responsible for coloration in amphibians and fluoresce in the near-infrared (NIR) spectral region. Here we produced the first functional recombinant BBS of the polka-dot treefrog Boana punctata (BpBBS), assembled with its biliverdin (BV) chromophore, and report its biochemical and photochemical characterization. We determined the crystal structure of BpBBS at 2.05 A resolution, which demonstrated its structural homology to the mammalian protease inhibitor alpha-1-antitrypsin. BV interaction with BpBBS was studied and it was found that the N-terminal polypeptide (residues 19-50) plays a critical role in the BV binding. By comparing BpBBS with the available NIR fluorescent proteins and expressing it in mammalian cells, we demonstrated its potential as a NIR imaging probe. These results provide insight into the non-inhibitory function of serpins, provide a basis for improving their performance in mammalian cells, and suggest possible paths for the development of BBS-based fluorescent probes. Structural and Functional Characterization of a Biliverdin-Binding Near-Infrared Fluorescent Protein From the Serpin Superfamily.,Manoilov KY, Ghosh A, Almo SC, Verkhusha VV J Mol Biol. 2021 Nov 16;434(2):167359. doi: 10.1016/j.jmb.2021.167359. PMID:34798132[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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