6ZZL
Crystal structure of the catalytic domain plus N-terminal linker of the acetyltransferase AceF (E2p) from Corynebacterium glutamicum.
Summary for 6ZZL
| Entry DOI | 10.2210/pdb6zzl/pdb |
| Descriptor | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, GLYCEROL, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | pdh, acetyltransferase, lipoamide, corynebacterium, coa, transferase |
| Biological source | Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) |
| Total number of polymer chains | 3 |
| Total formula weight | 99977.85 |
| Authors | Yang, L.,Bellinzoni, M. (deposition date: 2020-08-04, release date: 2021-08-18, Last modification date: 2024-01-31) |
| Primary citation | Bruch, E.M.,Vilela, P.,Yang, L.,Boyko, A.,Lexa-Sapart, N.,Raynal, B.,Alzari, P.M.,Bellinzoni, M. Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex. Proc.Natl.Acad.Sci.USA, 118:-, 2021 Cited by PubMed Abstract: α-oxoacid dehydrogenase complexes are large, tripartite enzymatic machineries carrying out key reactions in central metabolism. Extremely conserved across the tree of life, they have been, so far, all considered to be structured around a high-molecular weight hollow core, consisting of up to 60 subunits of the acyltransferase component. We provide here evidence that Actinobacteria break the rule by possessing an acetyltranferase component reduced to its minimally active, trimeric unit, characterized by a unique C-terminal helix bearing an actinobacterial specific insertion that precludes larger protein oligomerization. This particular feature, together with the presence of an gene coding for both the decarboxylase and the acyltransferase domains on the same polypetide, is spread over Actinobacteria and reflects the association of PDH and ODH into a single physical complex. Considering the central role of the pyruvate and 2-oxoglutarate nodes in central metabolism, our findings pave the way to both therapeutic and metabolic engineering applications. PubMed: 34819376DOI: 10.1073/pnas.2112107118 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.229 Å) |
Structure validation
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