View source for 6kgx


==Structure of the phycobilisome from the red alga Porphyridium purpureum==
<SX load='6kgx' size='340' side='right' viewer='molstar' caption='[[6kgx]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6kgx]] is a 632 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyridium_purpureum Porphyridium purpureum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KGX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene>, <scene name='pdbligand=MEN:N-METHYL+ASPARAGINE'>MEN</scene>, <scene name='pdbligand=PEB:PHYCOERYTHROBILIN'>PEB</scene>, <scene name='pdbligand=PUB:PHYCOUROBILIN'>PUB</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=6kgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kgx OCA], [https://pdbe.org/6kgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kgx RCSB], [https://www.ebi.ac.uk/pdbsum/6kgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kgx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E2IH77_PORPP E2IH77_PORPP] 
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== Publication Abstract from PubMed ==
Photosynthetic organisms have developed various light-harvesting systems to adapt to their environments(1). Phycobilisomes are large light-harvesting protein complexes found in cyanobacteria and red algae(2-4), although how the energies of the chromophores within these complexes are modulated by their environment is unclear. Here we report the cryo-electron microscopy structure of a 14.7-megadalton phycobilisome with a hemiellipsoidal shape from the red alga Porphyridium purpureum. Within this complex we determine the structures of 706 protein subunits, including 528 phycoerythrin, 72 phycocyanin, 46 allophycocyanin and 60 linker proteins. In addition, 1,598 chromophores are resolved comprising 1,430 phycoerythrobilin, 48 phycourobilin and 120 phycocyanobilin molecules. The markedly improved resolution of our structure compared with that of the phycobilisome of Griffithsia pacifica(5) enabled us to build an accurate atomic model of the P. purpureum phycobilisome system. The model reveals how the linker proteins affect the microenvironment of the chromophores, and suggests that interactions of the aromatic amino acids of the linker proteins with the chromophores may be a key factor in fine-tuning the energy states of the chromophores to ensure the efficient unidirectional transfer of energy.

Structural basis of energy transfer in Porphyridium purpureum phycobilisome.,Ma J, You X, Sun S, Wang X, Qin S, Sui SF Nature. 2020 Mar;579(7797):146-151. doi: 10.1038/s41586-020-2020-7. Epub 2020 Feb, 19. PMID:32076272<ref>PMID:32076272</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6kgx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Allophycocyanin 3D structures|Allophycocyanin 3D structures]]
*[[Phycocyanin|Phycocyanin]]
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Porphyridium purpureum]]
[[Category: Ma JF]]
[[Category: Sui SF]]
[[Category: Sun S]]
[[Category: You X]]