9TVK
Structure of the Tetrapod Ancestor COQ8B in complex with ADP and 2Mn(II)
Summary for 9TVK
| Entry DOI | 10.2210/pdb9tvk/pdb |
| Descriptor | Atypical kinase COQ8B, mitochondrial, ADENOSINE-5'-DIPHOSPHATE, MANGANESE (II) ION, ... (7 entities in total) |
| Functional Keywords | atpase, coenzymeq biosynthesis, atypical kinase, lipid binding protein, lipid transport |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 56339.99 |
| Authors | Gottinger, A.,Mattevi, A. (deposition date: 2026-01-12, release date: 2026-06-24, Last modification date: 2026-08-19) |
| Primary citation | Gottinger, A.,Malatesta, M.,Nicoll, C.R.,Ansari, G.,Quinodoz, M.,Kaminska, K.,Tang, R.W.C.,Tan, T.E.,Fenner, B.J.,Barberan-Martinez, P.,Garcia-Garcia, G.,Millan, J.M.,Pfau, M.,Burbach, N.E.,Cecchini, D.,Rivolta, C.,Mattevi, A. COQ8 chaperones coenzyme Q lipid intermediates through ATP-driven structural gating. Sci Adv, 12:eaeg1124-eaeg1124, 2026 Cited by PubMed Abstract: Coenzyme Q biosynthesis requires two atypical kinase-like proteins (COQ8A and COQ8B), whose detailed molecular mechanism remains unclear. Here, we show that both paralogs function as adenosine triphosphatases (ATPases) that promote coenzyme Q biosynthetic metabolon activity by engaging in loose protein-protein interactions and delivering insoluble biosynthetic intermediates. Structural bioinformatics and pathological variant-driven mutagenesis identify a previously uncharacterized pocket that selectively recognizes coenzyme Q biosynthetic intermediates via their head groups. X-ray crystallography reveals that access to this pocket is gated by long-range conformational changes controlled by adenosine 5'-triphosphate hydrolysis. Last, excess coenzyme Q suppresses binding of early-stage intermediates and thereby abolishes the promoting effect of COQ8 on the metabolon. Together, these findings support a model in which COQ8 tunes coenzyme Q biosynthesis by coupling ATPase-driven intermediate chaperoning to feedback inhibition by the final product. PubMed: 42525751DOI: 10.1126/sciadv.aeg1124 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.398 Å) |
Structure validation
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