6H05
Cryo-electron microscopic structure of the dihydrolipoamide succinyltransferase (E2) component of the human alpha-ketoglutarate (2-oxoglutarate) dehydrogenase complex [residues 218-453]
Summary for 6H05
| Entry DOI | 10.2210/pdb6h05/pdb |
| EMDB information | 0108 |
| Descriptor | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (1 entity in total) |
| Functional Keywords | alpha-ketoglutarate dehydrogenase complex; 2-oxoglutarate dehydrogenase complex; dihydrolipoamide succinyltransferase; e2 component, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 45543.00 |
| Authors | Nagy, B.,Zambo, Z.,Hubert, A.,Polak, M.,Nemeria, N.S.,Novacek, J.,Jordan, F.,Adam-Vizi, V.,Ambrus, A. (deposition date: 2018-07-06, release date: 2020-01-22, Last modification date: 2024-10-02) |
| Primary citation | Nagy, B.,Polak, M.,Ozohanics, O.,Zambo, Z.,Szabo, E.,Hubert, A.,Jordan, F.,Novacek, J.,Adam-Vizi, V.,Ambrus, A. Structure of the dihydrolipoamide succinyltransferase (E2) component of the human alpha-ketoglutarate dehydrogenase complex (hKGDHc) revealed by cryo-EM and cross-linking mass spectrometry: Implications for the overall hKGDHc structure. Biochim Biophys Acta Gen Subj, 1865:129889-129889, 2021 Cited by PubMed Abstract: The human mitochondrial alpha-ketoglutarate dehydrogenase complex (hKGDHc) converts KG to succinyl-CoA and NADH. Malfunction of and reactive oxygen species generation by the hKGDHc as well as its E1-E2 subcomplex are implicated in neurodegenerative disorders, ischemia-reperfusion injury, E3-deficiency and cancers. PubMed: 33684457DOI: 10.1016/j.bbagen.2021.129889 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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