8wcl: Difference between revisions
New page: '''Unreleased structure''' The entry 8wcl is ON HOLD Authors: Feng, Y., Li, Z., Zhou, C., Liu, C., Shen, J.-R., Wang, W. Description: FCP pentamer in Chaetoceros gracilis [[Category: U... |
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==FCP pentamer in Chaetoceros gracilis== | |||
<StructureSection load='8wcl' size='340' side='right'caption='[[8wcl]], [[Resolution|resolution]] 2.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8wcl]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetoceros_neogracilis Chaetoceros neogracilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WCL 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]] 2.65Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A86:(3S,3S,5R,5R,6S,6R,8R)-3,5-dihydroxy-8-oxo-6,7-didehydro-5,5,6,6,7,8-hexahydro-5,6-epoxy-beta,beta-caroten-3-+yl+acetate'>A86</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=KC1:Chlorophyll+c1'>KC1</scene>, <scene name='pdbligand=KC2:Chlorophyll+c2'>KC2</scene>, <scene name='pdbligand=LMG:1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE'>LMG</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</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=8wcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wcl OCA], [https://pdbe.org/8wcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wcl RCSB], [https://www.ebi.ac.uk/pdbsum/8wcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wcl ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Diatoms, a group of prevalent marine algae, significantly contribute to global primary productivity. Their substantial biomass is linked to enhanced absorption of blue-green light underwater, facilitated by fucoxanthin chlorophyll a/c-binding proteins (FCPs), exhibiting oligomeric diversity across diatom species. Utilizing mild CN-PAGE analysis on solubilized thylakoid membranes, we displayed monomeric, dimeric, trimeric, tetrameric and pentameric FCPs in diatoms. Mass spectrometry analysis revealed each oligomeric FCP has specific protein compositions, constituting a large Lhcf family of FCP antennas. In addition, we resolved the structures of Thalassiosira pseudonana FCP (Tp-FCP) homotrimer and Chaetoceros gracilis FCP (Cg-FCP) pentamer by cryo-electron microscopy at 2.73 A and 2.65 A resolutions, respectively. The distinct pigment composition and organization in various oligomeric FCPs change their blue-green light-harvesting, excitation energy transfer pathways. In comparison to dimeric and trimeric FCPs, Cg-FCP tetramer and Cg-FCP pentamer exhibit stronger absorption by Chls c, red-shifted and broader Chl a fluorescence emission, as well as more robust circular dichroism signals originating from Chl a-carotenoid dimers. These spectroscopic characteristics indicate that Chl a molecules in Cg-FCP tetramer and Cg-FCP pentamer are more heterogeneous than in both dimers and Tp-FCP trimer. The structural and spectroscopic insights provided by this study contribute to a better understanding of the mechanisms that empower diatoms to adapt to fluctuating light environments. | |||
Structural and spectroscopic insights into fucoxanthin chlorophyll a/c-binding proteins of diatoms in diverse oligomeric states.,Zhou C, Feng Y, Li Z, Shen L, Li X, Wang Y, Han G, Kuang T, Liu C, Shen JR, Wang W Plant Commun. 2024 Jul 17:101041. doi: 10.1016/j.xplc.2024.101041. PMID:39030906<ref>PMID:39030906</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8wcl" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Liu | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Chaetoceros neogracilis]] | ||
[[Category: Large Structures]] | |||
[[Category: Feng Y]] | |||
[[Category: Li Z]] | |||
[[Category: Liu C]] | |||
[[Category: Shen J-R]] | |||
[[Category: Wang W]] | |||
[[Category: Zhou C]] |
Latest revision as of 09:07, 31 July 2024
FCP pentamer in Chaetoceros gracilisFCP pentamer in Chaetoceros gracilis
Structural highlights
Publication Abstract from PubMedDiatoms, a group of prevalent marine algae, significantly contribute to global primary productivity. Their substantial biomass is linked to enhanced absorption of blue-green light underwater, facilitated by fucoxanthin chlorophyll a/c-binding proteins (FCPs), exhibiting oligomeric diversity across diatom species. Utilizing mild CN-PAGE analysis on solubilized thylakoid membranes, we displayed monomeric, dimeric, trimeric, tetrameric and pentameric FCPs in diatoms. Mass spectrometry analysis revealed each oligomeric FCP has specific protein compositions, constituting a large Lhcf family of FCP antennas. In addition, we resolved the structures of Thalassiosira pseudonana FCP (Tp-FCP) homotrimer and Chaetoceros gracilis FCP (Cg-FCP) pentamer by cryo-electron microscopy at 2.73 A and 2.65 A resolutions, respectively. The distinct pigment composition and organization in various oligomeric FCPs change their blue-green light-harvesting, excitation energy transfer pathways. In comparison to dimeric and trimeric FCPs, Cg-FCP tetramer and Cg-FCP pentamer exhibit stronger absorption by Chls c, red-shifted and broader Chl a fluorescence emission, as well as more robust circular dichroism signals originating from Chl a-carotenoid dimers. These spectroscopic characteristics indicate that Chl a molecules in Cg-FCP tetramer and Cg-FCP pentamer are more heterogeneous than in both dimers and Tp-FCP trimer. The structural and spectroscopic insights provided by this study contribute to a better understanding of the mechanisms that empower diatoms to adapt to fluctuating light environments. Structural and spectroscopic insights into fucoxanthin chlorophyll a/c-binding proteins of diatoms in diverse oligomeric states.,Zhou C, Feng Y, Li Z, Shen L, Li X, Wang Y, Han G, Kuang T, Liu C, Shen JR, Wang W Plant Commun. 2024 Jul 17:101041. doi: 10.1016/j.xplc.2024.101041. PMID:39030906[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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