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-Structure paper
Title | Dynamic Arabidopsis P5CS filament facilitates substrate channelling. |
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Journal, issue, pages | Nat Plants, Vol. 10, Issue 6, Page 880-889, Year 2024 |
Publish date | May 13, 2024 |
Authors | Chen-Jun Guo / Tianyi Zhang / Qingqing Leng / Xian Zhou / Jiale Zhong / Ji-Long Liu / |
PubMed Abstract | In plants, the rapid accumulation of proline is a common response to combat abiotic stress. Delta-1-pyrroline-5-carboxylate synthase (P5CS) is a rate-limiting enzyme in proline synthesis, catalysing ...In plants, the rapid accumulation of proline is a common response to combat abiotic stress. Delta-1-pyrroline-5-carboxylate synthase (P5CS) is a rate-limiting enzyme in proline synthesis, catalysing the initial two-step conversion from glutamate to proline. Here we determine the first structure of plant P5CS. Our results show that Arabidopsis thaliana P5CS1 (AtP5CS1) and P5CS2 (AtP5CS2) can form enzymatic filaments in a substrate-sensitive manner. The destruction of AtP5CS filaments by mutagenesis leads to a significant reduction in enzymatic activity. Furthermore, separate activity tests on two domains reveal that filament-based substrate channelling is essential for maintaining the high catalytic efficiency of AtP5CS. Our study demonstrates the unique mechanism for the efficient catalysis of AtP5CS, shedding light on the intricate mechanisms underlying plant proline metabolism and stress response. |
External links | Nat Plants / PubMed:38740943 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.3 Å |
Structure data | EMDB-35901, PDB-8j0f: EMDB-38855, PDB-8y2h: |
Chemicals | ChemComp-ADP: ChemComp-RGP: ChemComp-MG: ChemComp-ATP: |
Source |
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Keywords | PLANT PROTEIN / L-proline biosynthesis / filamentous enzyme / TRANSFERASE |