7z6q: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7z6q]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorobaculum_tepidum_TLS Chlorobaculum tepidum TLS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z6Q FirstGlance]. <br>
<table><tr><td colspan='2'>[[7z6q]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorobaculum_tepidum_TLS Chlorobaculum tepidum TLS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z6Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z6Q 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>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=F39:[(2R,3S,4S,5R,6R)-6-[(10E,12E,14E)-2,6,10,14,19,23-hexamethyl-25-(2,3,6-trimethylphenyl)pentacosa-6,8,10,12,14,16,18,20,22,24-decaen-2-yl]oxy-3,4,5-tris(oxidanyl)oxan-2-yl]methyl+dodecanoate'>F39</scene>, <scene name='pdbligand=GS0:Bacteriochlorophyll+A+isomer'>GS0</scene>, <scene name='pdbligand=IKV:[(2~{R})-2-hexadecanoyloxy-3-[(2~{S},3~{S},4~{R},5~{R},6~{S})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-propyl]+hexadecanoate'>IKV</scene>, <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</scene>, <scene name='pdbligand=F39:[(2~{R},3~{S},4~{S},5~{R},6~{R})-6-[(10~{E},12~{E},14~{E})-2,6,10,14,19,23-hexamethyl-25-(2,3,6-trimethylphenyl)pentacosa-6,8,10,12,14,16,18,20,22,24-decaen-2-yl]oxy-3,4,5-tris(oxidanyl)oxan-2-yl]methyl+dodecanoate'>F39</scene>, <scene name='pdbligand=IKV:[(2~{R})-2-hexadecanoyloxy-3-[(2~{S},3~{S},4~{R},5~{R},6~{S})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-propyl]+hexadecanoate'>IKV</scene>, <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</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=7z6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z6q OCA], [https://pdbe.org/7z6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z6q RCSB], [https://www.ebi.ac.uk/pdbsum/7z6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z6q 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=7z6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z6q OCA], [https://pdbe.org/7z6q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z6q RCSB], [https://www.ebi.ac.uk/pdbsum/7z6q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z6q ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q8KAY0_CHLTE Q8KAY0_CHLTE]  
[https://www.uniprot.org/uniprot/Q8KAY0_CHLTE Q8KAY0_CHLTE]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Light energy absorption and transfer are very important processes in photosynthesis. In green sulfur bacteria light is absorbed primarily by the chlorosomes and its energy is transferred via the Fenna-Matthews-Olson (FMO) proteins to a homodimeric reaction center (RC). Here, we report the cryogenic electron microscopic structure of the intact FMO-RC apparatus from Chlorobaculum tepidum at 2.5 A resolution. The FMO-RC apparatus presents an asymmetric architecture and contains two FMO trimers that show different interaction patterns with the RC core. Furthermore, the two permanently bound transmembrane subunits PscC, which donate electrons to the special pair, interact only with the two large PscA subunits. This structure fills an important gap in our understanding of the transfer of energy from antenna to the electron transport chain of this RC and the transfer of electrons from reduced sulfur compounds to the special pair.
Cryo-EM structure of the whole photosynthetic reaction center apparatus from the green sulfur bacterium Chlorobaculum tepidum.,Xie H, Lyratzakis A, Khera R, Koutantou M, Welsch S, Michel H, Tsiotis G Proc Natl Acad Sci U S A. 2023 Jan 31;120(5):e2216734120. doi: , 10.1073/pnas.2216734120. Epub 2023 Jan 24. PMID:36693097<ref>PMID:36693097</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7z6q" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
</StructureSection>
Retrieved from "https://proteopedia.org/7z6q"