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8ZRO

Arabidopsis Carboxylesterase CXE15

Summary for 8ZRO
Entry DOI10.2210/pdb8zro/pdb
Related8ZR6
DescriptorStrigolactones hydrolase CXE15 (1 entity in total)
Functional Keywordscatabolic enzyme, cxe15, strigolactoone, carboxylesterase, hydrolase
Biological sourceArabidopsis thaliana (thale cress)
Total number of polymer chains2
Total formula weight71670.73
Authors
Arold, S.T.,Hameed, U.F.S. (deposition date: 2024-06-05, release date: 2025-05-28, Last modification date: 2025-12-03)
Primary citationShahul Hameed, U.F.,Balakrishna, A.,Wang, J.Y.,Alvarez, D.,Momin, A.A.,Schwarzenberg, A.,Al-Babili, S.,Arold, S.T.
Molecular Basis for Catalysis and Regulation of the Strigolactone Catabolic Enzyme CXE15.
Nat Commun, 16:10290-10290, 2025
Cited by
PubMed Abstract: Strigolactones (SLs) are pivotal plant hormones involved in developmental, physiological, and adaptive processes. SLs also facilitate symbiosis with arbuscular mycorrhizal fungi and trigger germination of root parasitic Striga plants. The carboxylesterase CXE15, recently identified as the SL catabolic enzyme in Arabidopsis thaliana, plays a crucial role in regulating SL levels. Our study elucidates the structural and regulatory mechanisms of CXE15. We present four crystal structures capturing the conformational dynamics of CXE15, revealing a unique N-terminal extension (Nt) that transitions from a β-sheet in monomers to an intertwined helical structure in dimers. Only the dimeric form is catalytically active, as it forms a hydrophobic cavity for SLs between its two active sites. The moderate dimerisation affinity allows for genetic regulation through protein expression levels. Additionally, we identify an environment-controlled regulation mechanism. Under oxidising conditions, a disulphide bond forms between Cys14 of the two monomers, blocking the active site and inhibiting SL cleavage. This redox-sensitive inhibition of SL catabolism, triggered by reactive oxygen species (ROS) in response to abiotic stress, suggests a mechanism for maintaining high SL levels under beneficial conditions. Our findings provide molecular insights into the regulation of SL homeostasis and catabolism under stress conditions.
PubMed: 41271671
DOI: 10.1038/s41467-025-65204-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.09 Å)
Structure validation

246031

数据于2025-12-10公开中

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