4jdq: Difference between revisions
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==Structure of the Fluorescence Recovery Protein from Synechocystis sp PCC 6803, R60K mutant== | ==Structure of the Fluorescence Recovery Protein from Synechocystis sp PCC 6803, R60K mutant== | ||
<StructureSection load='4jdq' size='340' side='right' caption='[[4jdq]], [[Resolution|resolution]] 3.52Å' scene=''> | <StructureSection load='4jdq' size='340' side='right'caption='[[4jdq]], [[Resolution|resolution]] 3.52Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jdq]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4jdq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JDQ FirstGlance]. <br> | ||
</td></tr> | </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=4jdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jdq OCA], [https://pdbe.org/4jdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jdq RCSB], [https://www.ebi.ac.uk/pdbsum/4jdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jdq ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/FRP_SYNY3 FRP_SYNY3] Destabilizes orange carotenoid protein-R form (OCP-R), the FRP-OCP interaction accelerates the OCP-R to OCP-O conversion (PubMed:20534537, PubMed:23716688). Increases fluorescence recovery following non-photochemical quenching (NPQ) by OCP, most probably by destabilizing OCP-R binding to the phycobilisome core (PubMed:21764991).<ref>PMID:20534537</ref> <ref>PMID:21764991</ref> <ref>PMID:23716688</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synechocystis sp. PCC 6803 substr. Kazusa]] | ||
[[Category: | [[Category: Kerfeld CA]] | ||
[[Category: | [[Category: Sutter M]] | ||
Revision as of 14:08, 24 November 2022
Structure of the Fluorescence Recovery Protein from Synechocystis sp PCC 6803, R60K mutantStructure of the Fluorescence Recovery Protein from Synechocystis sp PCC 6803, R60K mutant
Structural highlights
FunctionFRP_SYNY3 Destabilizes orange carotenoid protein-R form (OCP-R), the FRP-OCP interaction accelerates the OCP-R to OCP-O conversion (PubMed:20534537, PubMed:23716688). Increases fluorescence recovery following non-photochemical quenching (NPQ) by OCP, most probably by destabilizing OCP-R binding to the phycobilisome core (PubMed:21764991).[1] [2] [3] Publication Abstract from PubMedPhotosynthetic reaction centers are sensitive to high light conditions, which can cause damage because of the formation of reactive oxygen species. To prevent high-light induced damage, cyanobacteria have developed photoprotective mechanisms. One involves a photoactive carotenoid protein that decreases the transfer of excess energy to the reaction centers. This protein, the orange carotenoid protein (OCP), is present in most cyanobacterial strains; it is activated by high light conditions and able to dissipate excess energy at the site of the light-harvesting antennae, the phycobilisomes. Restoration of normal antenna capacity involves the fluorescence recovery protein (FRP). The FRP acts to dissociate the OCP from the phycobilisomes by accelerating the conversion of the active red OCP to the inactive orange form. We have determined the 3D crystal structure of the FRP at 2.5 A resolution. Remarkably, the FRP is found in two very different conformational and oligomeric states in the same crystal. Based on amino acid conservation analysis, activity assays of FRP mutants, FRP:OCP docking simulations, and coimmunoprecipitation experiments, we conclude that the dimer is the active form. The second form, a tetramer, may be an inactive form of FRP. In addition, we have identified a surface patch of highly conserved residues and shown that those residues are essential to FRP activity. Crystal structure of the FRP and identification of the active site for modulation of OCP-mediated photoprotection in cyanobacteria.,Sutter M, Wilson A, Leverenz RL, Lopez-Igual R, Thurotte A, Salmeen AE, Kirilovsky D, Kerfeld CA Proc Natl Acad Sci U S A. 2013 May 28. PMID:23716688[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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