9G7F
Cryo-EM structure of Acetyl-coenzyme A synthetase (AcsA) dimer
Summary for 9G7F
| Entry DOI | 10.2210/pdb9g7f/pdb |
| Related | 9G79 |
| EMDB information | 51121 5116 |
| Descriptor | Acetyl-coenzyme A synthetase, Acetoin utilization protein AcuA (2 entities in total) |
| Functional Keywords | ac-coa synthetase acsa, acetate switch, gcn5-related n-acetyltransferase acua, biosynthetic protein |
| Biological source | Bacillus subtilis More |
| Total number of polymer chains | 3 |
| Total formula weight | 154314.45 |
| Authors | |
| Primary citation | Zheng, L.,Du, Y.,Steinchen, W.,Girbig, M.,Abendroth, F.,Jalomo-Khayrova, E.,Bedrunka, P.,Bekeredjian-Ding, I.,Mais, C.N.,Hochberg, G.K.A.,Freitag, J.,Bange, G. Regulation of acetyl-CoA biosynthesis via an intertwined acetyl-CoA synthetase/acetyltransferase complex. Nat Commun, 16:2557-2557, 2025 Cited by PubMed Abstract: Acetyl-CoA synthetase (Acs) generates acetyl-coenzyme A (Ac-CoA) but its excessive activity can deplete ATP and lead to a growth arrest. To prevent this, Acs is regulated through Ac-CoA-dependent feedback inhibition executed by Ac-CoA-dependent acetyltransferases such as AcuA in Bacillus subtilis. AcuA acetylates the catalytic lysine of AcsA turning the synthetase inactive. Here, we report that AcuA and AcsA form a tightly intertwined complex - the C-terminal domain binds to acetyltransferase domain of AcuA, while the C-terminus of AcuA occupies the CoA-binding site in the N-terminal domain of AcsA. Formation of the complex reduces AcsA activity in addition to the well-established acetylation of the catalytic lysine 549 in AcsA which we show can disrupt the complex. Thus, different modes of regulation accomplished through AcuA adjust AcsA activity to the concentrations of the different substrates of the reaction. In summary, our study provides detailed mechanistic insights into the regulatory framework underlying acetyl-CoA biosynthesis from acetate. PubMed: 40089509DOI: 10.1038/s41467-025-57842-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.93 Å) |
Structure validation
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