9KPR
Crystal structure of a allulose transcriptional regulator from Agrobacterium fabrum
This is a non-PDB format compatible entry.
Summary for 9KPR
| Entry DOI | 10.2210/pdb9kpr/pdb |
| Descriptor | Transcriptional regulator, LacI family, D-Allulose (3 entities in total) |
| Functional Keywords | catalysis, transcription |
| Biological source | Agrobacterium fabrum str. C58 |
| Total number of polymer chains | 2 |
| Total formula weight | 79369.91 |
| Authors | Wei, H.L.,Dong, Q.Z.,Liu, W.D.,Yang, J.G.,Sun, Y.X. (deposition date: 2024-11-24, release date: 2025-11-26, Last modification date: 2026-01-14) |
| Primary citation | Dong, Q.,Chen, P.,Guo, Z.,Wei, H.,Zeng, Y.,Zhang, J.,Men, Y.,Liu, W.,Sun, Y.,Yang, J. Computational design of allulose-responsive biosensor toolbox for auto-inducible protein expression and CRISPRi mediated dynamic metabolic regulation. Nat Commun, 16:11562-11562, 2025 Cited by PubMed Abstract: Biosensors based on transcription factors (TFs) have shown extensive applications in synthetic biology. Due to the complex multi-domain structure of effector-TF-DNA, computational design of TFs remains a challenge. Here, we present the successful structure-guided computational design of the access tunnel, ligand binding, allosteric transition process for an allulose-responsive PsiR. It enables a 20-fold increase in sensitivity, reducing the EC of PsiR-allulose biosensors (PABs) from 16 mM to 0.8 mM, and delivers a PAB box possessing the detection range from 10 μM to 100 mM. We further validate its broader applicability in enhancing sensitivity of LacI-IPTG biosensor. Based on the developed PABs, we present the inducer-free allulose-mediated auto-inducible protein expression system, and demonstrate an allulose-triggered CRISPR interference circuit for dynamic metabolic regulation. It facilitates a 68% increase in allulose titer and achieves a high yield of 0.43 g/g glucose. This work provides the versatile TF toolbox for developing allulose-triggered regulation circuits in biotechnology application. PubMed: 41430049DOI: 10.1038/s41467-025-67669-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.53 Å) |
Structure validation
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