8RP0
Aminodeoxychorismate synthase complex from Escherichia coli, with glutamine and chorismate added
This is a non-PDB format compatible entry.
Summary for 8RP0
| Entry DOI | 10.2210/pdb8rp0/pdb |
| Descriptor | Aminodeoxychorismate synthase component 2, Aminodeoxychorismate synthase component 1, GLUTAMIC ACID, ... (10 entities in total) |
| Functional Keywords | glutamine amidotransferase folate biosynthesis, transferase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 146618.85 |
| Authors | Sung, S.,Funke, F.J.,Schlee, S.,Sterner, R.,Wilmanns, M. (deposition date: 2024-01-12, release date: 2025-01-29, Last modification date: 2025-05-28) |
| Primary citation | Funke, F.J.,Schlee, S.,Bento, I.,Bourenkov, G.,Sterner, R.,Wilmanns, M. Activity Regulation of a Glutamine Amidotransferase Bienzyme Complex by Substrate-Induced Subunit Interface Expansion. Acs Catalysis, 15:4359-4373, 2025 Cited by PubMed Abstract: Glutamine amidotransferases are multienzyme machineries in which reactive ammonia is generated by a glutaminase and then transferred through a sequestered protein tunnel to a synthase active site for incorporation into diverse metabolites. To avoid wasteful metabolite consumption, there is a requirement for synchronized catalysis, but any generally applicable mechanistic insight is still lacking. As synthase activity depends on glutamine turnover, we investigated possible mechanisms controlling glutaminase catalysis using aminodeoxychorismate synthase involved in folate biosynthesis as a model. By analyzing this system in distinct states of catalysis, we found that incubation with glutamine leads to a subunit interface expansion by one-third of its original area. These changes completely enclose the glutaminase active site for sequestered catalysis and the subsequent transport of volatile ammonia to the synthase active site. In view of similar rearrangements in other glutamine amidotransferases, our observations may provide a general mechanism for the catalysis synchronization of this multienzyme family. PubMed: 40365074DOI: 10.1021/acscatal.4c07438 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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