8to2: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8to2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8to2 OCA], [https://pdbe.org/8to2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8to2 RCSB], [https://www.ebi.ac.uk/pdbsum/8to2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8to2 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=8to2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8to2 OCA], [https://pdbe.org/8to2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8to2 RCSB], [https://www.ebi.ac.uk/pdbsum/8to2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8to2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
<div style="background-color:#fffaf0;">
[https://www.uniprot.org/uniprot/APCE_SYNY3 APCE_SYNY3] This protein is postulated to act both as terminal energy acceptor (by its phycobilin-like domains) and as a linker polypeptide (by its repeats and arms) that stabilizes the phycobilisome core architecture. Has intrinsic bilin lyase activity (By similarity).
== Publication Abstract from PubMed ==
Cyanobacteria use large antenna complexes called phycobilisomes (PBSs) for light harvesting. However, intense light triggers non-photochemical quenching, where the orange carotenoid protein (OCP) binds to PBS, dissipating excess energy as heat. The mechanism of efficiently transferring energy from phycocyanobilins in PBS to canthaxanthin in OCP remains insufficiently understood. Using cryo-electron microscopy, we unveiled the OCP-PBS complex structure at 1.6- to 2.1-angstrom resolution, showcasing its inherent flexibility. Using multiscale quantum chemistry, we disclosed the quenching mechanism. Identifying key protein residues, we clarified how canthaxanthin's transition dipole moment in its lowest-energy dark state becomes large enough for efficient energy transfer from phycocyanobilins. Our energy transfer model offers a detailed understanding of the atomic determinants of light harvesting regulation and antenna architecture in cyanobacteria.
 
Structural and quantum chemical basis for OCP-mediated quenching of phycobilisomes.,Sauer PV, Cupellini L, Sutter M, Bondanza M, Dominguez Martin MA, Kirst H, Bina D, Koh AF, Kotecha A, Greber BJ, Nogales E, Polivka T, Mennucci B, Kerfeld CA Sci Adv. 2024 Apr 5;10(14):eadk7535. doi: 10.1126/sciadv.adk7535. Epub 2024 Apr , 5. PMID:38578996<ref>PMID:38578996</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8to2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 13:01, 9 October 2024

Bottom cylinder of high-resolution phycobilisome quenched by OCP (local refinement)Bottom cylinder of high-resolution phycobilisome quenched by OCP (local refinement)

Structural highlights

8to2 is a 29 chain structure with sequence from Synechocystis sp. PCC 6803. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Cyanobacteria use large antenna complexes called phycobilisomes (PBSs) for light harvesting. However, intense light triggers non-photochemical quenching, where the orange carotenoid protein (OCP) binds to PBS, dissipating excess energy as heat. The mechanism of efficiently transferring energy from phycocyanobilins in PBS to canthaxanthin in OCP remains insufficiently understood. Using cryo-electron microscopy, we unveiled the OCP-PBS complex structure at 1.6- to 2.1-angstrom resolution, showcasing its inherent flexibility. Using multiscale quantum chemistry, we disclosed the quenching mechanism. Identifying key protein residues, we clarified how canthaxanthin's transition dipole moment in its lowest-energy dark state becomes large enough for efficient energy transfer from phycocyanobilins. Our energy transfer model offers a detailed understanding of the atomic determinants of light harvesting regulation and antenna architecture in cyanobacteria.

Structural and quantum chemical basis for OCP-mediated quenching of phycobilisomes.,Sauer PV, Cupellini L, Sutter M, Bondanza M, Dominguez Martin MA, Kirst H, Bina D, Koh AF, Kotecha A, Greber BJ, Nogales E, Polivka T, Mennucci B, Kerfeld CA Sci Adv. 2024 Apr 5;10(14):eadk7535. doi: 10.1126/sciadv.adk7535. Epub 2024 Apr , 5. PMID:38578996[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Sauer PV, Cupellini L, Sutter M, Bondanza M, Domínguez Martin MA, Kirst H, Bína D, Koh AF, Kotecha A, Greber BJ, Nogales E, Polívka T, Mennucci B, Kerfeld CA. Structural and quantum chemical basis for OCP-mediated quenching of phycobilisomes. Sci Adv. 2024 Apr 5;10(14):eadk7535. PMID:38578996 doi:10.1126/sciadv.adk7535

8to2, resolution 2.00Å

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OCA
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