6ZLM
Dihydrolipoyllysine-residue acetyltransferase component of fungal pyruvate dehydrogenase complex with protein X bound
This is a non-PDB format compatible entry.
Summary for 6ZLM
| Entry DOI | 10.2210/pdb6zlm/pdb |
| EMDB information | 11266 11267 11268 |
| Descriptor | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial, Pyruvate dehydrogenase X component (2 entities in total) |
| Functional Keywords | acetyl transferase, pyruvate dehydrogenase, protein complex, mitochondria, metabolism, tetrahedral icosahedral, transferase |
| Biological source | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) More |
| Total number of polymer chains | 72 |
| Total formula weight | 2934136.24 |
| Authors | Forsberg, B.O.,Aibara, S.,Howard, R.J.,Mortezaei, N.,Lindahl, E. (deposition date: 2020-06-30, release date: 2020-09-23, Last modification date: 2024-05-01) |
| Primary citation | Forsberg, B.O.,Aibara, S.,Howard, R.J.,Mortezaei, N.,Lindahl, E. Arrangement and symmetry of the fungal E3BP-containing core of the pyruvate dehydrogenase complex. Nat Commun, 11:4667-4667, 2020 Cited by PubMed Abstract: The pyruvate dehydrogenase complex (PDC) is a multienzyme complex central to aerobic respiration, connecting glycolysis to mitochondrial oxidation of pyruvate. Similar to the E3-binding protein (E3BP) of mammalian PDC, PX selectively recruits E3 to the fungal PDC, but its divergent sequence suggests a distinct structural mechanism. Here, we report reconstructions of PDC from the filamentous fungus Neurospora crassa by cryo-electron microscopy, where we find protein X (PX) interior to the PDC core as opposed to substituting E2 core subunits as in mammals. Steric occlusion limits PX binding, resulting in predominantly tetrahedral symmetry, explaining previous observations in Saccharomyces cerevisiae. The PX-binding site is conserved in (and specific to) fungi, and complements possible C-terminal binding motifs in PX that are absent in mammalian E3BP. Consideration of multiple symmetries thus reveals a differential structural basis for E3BP-like function in fungal PDC. PubMed: 32938938DOI: 10.1038/s41467-020-18401-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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