Protein community member pyruvate dehydrogenase complex E2 core from C. thermophilumProtein community member pyruvate dehydrogenase complex E2 core from C. thermophilum

Structural highlights

7q5r is a 60 chain structure with sequence from Chaetomium thermophilum (strain dsm 1495 / cbs 144.50 / imi 039719). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:Dihydrolipoyllysine-residue acetyltransferase, with EC number 2.3.1.12
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[G0S4X6_CHATD] The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).[RuleBase:RU361137]

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Skalidis I, Kyrilis FL, Tuting C, Hamdi F, Chojnowski G, Kastritis PL. Cryo-EM and artificial intelligence visualize endogenous protein community members. Structure. 2022 Jan 19. pii: S0969-2126(22)00001-6. doi:, 10.1016/j.str.2022.01.001. PMID:35093201 doi:http://dx.doi.org/10.1016/j.str.2022.01.001

7q5r, resolution 3.84Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA