EMD-37966

Subtomogram averaging
9.7 Å
EMD-37966 Deposition: 03/11/2023
Map released: 30/10/2024
Last modified: 30/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-37966

E1 of 2-oxoglutarate dehydrogenase complex subtomogram averaging map

EMD-37966

Subtomogram averaging
9.7 Å
EMD-37966 Deposition: 03/11/2023
Map released: 30/10/2024
Last modified: 30/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Sus scrofa
Sample: mitochondrial complex E1o subunit

Deposition Authors: Zhang SS, Zhang YT
Molecular architecture of the mammalian 2-oxoglutarate dehydrogenase complex.
Zhang Y , Chen M , Chen X , Zhang M , Yin J, Yang Z, Gao X , Zhang S , Yang M
(2024) Nat Commun , 15 , 8407 - 8407
PUBMED: 39333186
DOI: doi:10.1038/s41467-024-52792-7
ISSN: 2041-1723
Abstract:
The 2-oxoglutarate dehydrogenase complex (OGDHc) orchestrates a critical reaction regulating the TCA cycle. Although the structure of each OGDHc subunit has been solved, the architecture of the intact complex and inter-subunit interactions still remain unknown. Here we report the assembly of native, intact OGDHc from Sus scrofa heart tissue using cryo-electron microscopy (cryo-EM), cryo-electron tomography (cryo-ET), and subtomogram averaging (STA) to discern native structures of the whole complex and each subunit. Our cryo-EM analyses revealed the E2o cubic core structure comprising eight homotrimers at 3.3-Å resolution. More importantly, the numbers, positions and orientations of each OGDHc subunit were determined by cryo-ET and the STA structures of the core were resolved at 7.9-Å with the peripheral subunits reaching nanometer resolution. Although the distribution of the peripheral subunits E1o and E3 vary among complexes, they demonstrate a certain regularity within the position and orientation. Moreover, we analyzed and validated the interactions between each subunit, and determined the flexible binding mode for E1o, E2o and E3, resulting in a proposed model of Sus scrofa OGDHc. Together, our results reveal distinctive factors driving the architecture of the intact, native OGDHc.