7Q5Q
Protein community member oxoglutarate dehydrogenase complex E2 core from C. thermophilum
Summary for 7Q5Q
| Entry DOI | 10.2210/pdb7q5q/pdb |
| EMDB information | 13844 |
| Descriptor | Dihydrolipoyllysine-residue succinyltransferase (1 entity in total) |
| Functional Keywords | dihydrolipoyl succinyltransferase, e2, oxoglutarate, a-ketoglutarate, transferase |
| Biological source | Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) |
| Total number of polymer chains | 24 |
| Total formula weight | 1103688.10 |
| Authors | Chojnowski, G.,Skalidis, I.,Kyrilis, F.L.,Tueting, C.,Hamdi, F.,Kastritis, P.L. (deposition date: 2021-11-04, release date: 2022-02-02, Last modification date: 2023-12-13) |
| Primary citation | Skalidis, I.,Kyrilis, F.L.,Tuting, C.,Hamdi, F.,Chojnowski, G.,Kastritis, P.L. Cryo-EM and artificial intelligence visualize endogenous protein community members. Structure, 30:575-, 2022 Cited by PubMed Abstract: 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 Å 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. PubMed: 35093201DOI: 10.1016/j.str.2022.01.001 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.38 Å) |
Structure validation
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