5lcb
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5lcb]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorobaculum_tepidum_TLS Chlorobaculum tepidum TLS]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LCB FirstGlance]. <br> | <table><tr><td colspan='2'>[[5lcb]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorobaculum_tepidum_TLS Chlorobaculum tepidum TLS]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LCB FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy , Hybrid , Solid-state NMR, [[Resolution|Resolution]] 26.5Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</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=5lcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lcb OCA], [https://pdbe.org/5lcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lcb RCSB], [https://www.ebi.ac.uk/pdbsum/5lcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lcb 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=5lcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lcb OCA], [https://pdbe.org/5lcb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lcb RCSB], [https://www.ebi.ac.uk/pdbsum/5lcb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lcb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CSMA_CHLTE CSMA_CHLTE] Component of the photosynthetic apparatus. The light harvesting B740 complex binds bacteriochlorophyll c. | [https://www.uniprot.org/uniprot/CSMA_CHLTE CSMA_CHLTE] Component of the photosynthetic apparatus. The light harvesting B740 complex binds bacteriochlorophyll c. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Photosynthetic antenna systems enable organisms harvesting light and transfer the energy to the photosynthetic reaction centre, where the conversion to chemical energy takes place. One of the most complex antenna systems, the chlorosome, found in the photosynthetic green sulfur bacterium Chlorobaculum (Cba.) tepidum contains a baseplate, which is a scaffolding super-structure, formed by the protein CsmA and bacteriochlorophyll a. Here we present the first high-resolution structure of the CsmA baseplate using intact fully functional, light-harvesting organelles from Cba. tepidum, following a hybrid approach combining five complementary methods: solid-state NMR spectroscopy, cryo-electron microscopy, isotropic and anisotropic circular dichroism and linear dichroism. The structure calculation was facilitated through development of new software, GASyCS for efficient geometry optimization of highly symmetric oligomeric structures. We show that the baseplate is composed of rods of repeated dimers of the strongly amphipathic CsmA with pigments sandwiched within the dimer at the hydrophobic side of the helix. | ||
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| - | In situ high-resolution structure of the baseplate antenna complex in Chlorobaculum tepidum.,Nielsen JT, Kulminskaya NV, Bjerring M, Linnanto JM, Ratsep M, Pedersen MO, Lambrev PH, Dorogi M, Garab G, Thomsen K, Jegerschold C, Frigaard NU, Lindahl M, Nielsen NC Nat Commun. 2016 Aug 18;7:12454. doi: 10.1038/ncomms12454. PMID:27534696<ref>PMID:27534696</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 5lcb" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
Revision as of 16:02, 14 March 2024
In situ atomic-resolution structure of the baseplate antenna complex in Chlorobaculum tepidum obtained combining solid-state NMR spectroscopy, cryo electron microscopy and polarization spectroscopy
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