7q5r: Difference between revisions
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==Protein community member pyruvate dehydrogenase complex E2 core from C. thermophilum== | ==Protein community member pyruvate dehydrogenase complex E2 core from C. thermophilum== | ||
<StructureSection load='7q5r' size='340' side='right'caption='[[7q5r]]' scene=''> | <StructureSection load='7q5r' size='340' side='right'caption='[[7q5r]], [[Resolution|resolution]] 3.84Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q5R FirstGlance]. <br> | <table><tr><td colspan='2'>[[7q5r]] is a 60 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_(strain_dsm_1495_/_cbs_144.50_/_imi_039719) Chaetomium thermophilum (strain dsm 1495 / cbs 144.50 / imi 039719)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Q5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Q5R FirstGlance]. <br> | ||
</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=7q5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q5r OCA], [https://pdbe.org/7q5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q5r RCSB], [https://www.ebi.ac.uk/pdbsum/7q5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q5r ProSAT]</span></td></tr> | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrolipoyllysine-residue_acetyltransferase Dihydrolipoyllysine-residue acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.12 2.3.1.12] </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=7q5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7q5r OCA], [https://pdbe.org/7q5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7q5r RCSB], [https://www.ebi.ac.uk/pdbsum/7q5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7q5r ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/G0S4X6_CHATD G0S4X6_CHATD]] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).[RuleBase:RU361137] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cellular function is underlined by megadalton assemblies organizing in proximity, forming communities. Metabolons are protein communities involving metabolic pathways such as protein, fatty acid, and thioesters of coenzyme-A synthesis. Metabolons are highly heterogeneous due to their function, making their analysis particularly challenging. Here, we simultaneously characterize metabolon-embedded architectures of a 60S pre-ribosome, fatty acid synthase, and pyruvate/oxoglutarate dehydrogenase complex E2 cores de novo. Cryo-electron microscopy (cryo-EM) 3D reconstructions are resolved at 3.84-4.52 A resolution by collecting <3,000 micrographs of a single cellular fraction. After combining cryo-EM with artificial intelligence-based atomic modeling and de novo sequence identification methods, at this resolution range, polypeptide hydrogen bonding patterns are discernible. Residing molecular components resemble their purified counterparts from other eukaryotes but also exhibit substantial conformational variation with potential functional implications. Our results propose an integrated tool, boosted by machine learning, that opens doors for structural systems biology spearheaded by cryo-EM characterization of native cell extracts. | |||
Cryo-EM and artificial intelligence visualize endogenous protein community members.,Skalidis I, Kyrilis FL, Tuting C, Hamdi F, Chojnowski G, Kastritis PL Structure. 2022 Jan 19. pii: S0969-2126(22)00001-6. doi:, 10.1016/j.str.2022.01.001. PMID:35093201<ref>PMID:35093201</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7q5r" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Dihydrolipoyllysine-residue acetyltransferase]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chojnowski G]] | [[Category: Chojnowski, G]] | ||
[[Category: Hamdi F]] | [[Category: Hamdi, F]] | ||
[[Category: Kastritis | [[Category: Kastritis, P L]] | ||
[[Category: Kyrilis | [[Category: Kyrilis, F L]] | ||
[[Category: Skalidis I]] | [[Category: Skalidis, I]] | ||
[[Category: Tueting C]] | [[Category: Tueting, C]] | ||
[[Category: Dihydrolipoyl]] | |||
[[Category: E2]] | |||
[[Category: Pyruvate]] | |||
[[Category: Transacetylase]] | |||
[[Category: Transferase]] | |||