6YS6
Arabidopsis aspartate transcarbamoylase complex with PALA
Summary for 6YS6
| Entry DOI | 10.2210/pdb6ys6/pdb |
| Descriptor | PYRB, SULFATE ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | transferase, chloroplast, pyrimidine de novo biosynthesis, plant protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 3 |
| Total formula weight | 112845.52 |
| Authors | Ramon Maiques, S.,Del Cano Ochoa, F.,Bellin, L.,Mohlmann, T. (deposition date: 2020-04-21, release date: 2021-03-03, Last modification date: 2024-01-24) |
| Primary citation | Bellin, L.,Del Cano-Ochoa, F.,Velazquez-Campoy, A.,Mohlmann, T.,Ramon-Maiques, S. Mechanisms of feedback inhibition and sequential firing of active sites in plant aspartate transcarbamoylase. Nat Commun, 12:947-947, 2021 Cited by PubMed Abstract: Aspartate transcarbamoylase (ATC), an essential enzyme for de novo pyrimidine biosynthesis, is uniquely regulated in plants by feedback inhibition of uridine 5-monophosphate (UMP). Despite its importance in plant growth, the structure of this UMP-controlled ATC and the regulatory mechanism remain unknown. Here, we report the crystal structures of Arabidopsis ATC trimer free and bound to UMP, complexed to a transition-state analog or bearing a mutation that turns the enzyme insensitive to UMP. We found that UMP binds and blocks the ATC active site, directly competing with the binding of the substrates. We also prove that UMP recognition relies on a loop exclusively conserved in plants that is also responsible for the sequential firing of the active sites. In this work, we describe unique regulatory and catalytic properties of plant ATCs that could be exploited to modulate de novo pyrimidine synthesis and plant growth. PubMed: 33574254DOI: 10.1038/s41467-021-21165-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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