8VCA

Crystal Structure of plant Carboxylesterase 15

8VCA の概要

• エントリーDOI: 10.2210/pdb8vca/pdb
• 分子名称: Carboxylesterase 15, GLYCEROL (3 entities in total)
• 機能のキーワード: carboxylesterase 15, cxe15, strigolactone, hydrolase
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36912.52

構造登録者

Palayam, M.,Shabek, N. (登録日: 2023-12-13, 公開日: 2024-08-07, 最終更新日: 2024-08-14)

主引用文献

Palayam, M.,Yan, L.,Nagalakshmi, U.,Gilio, A.K.,Cornu, D.,Boyer, F.D.,Dinesh-Kumar, S.P.,Shabek, N.
Structural insights into strigolactone catabolism by carboxylesterases reveal a conserved conformational regulation.
Nat Commun, 15:6500-6500, 2024

PubMed Abstract: Phytohormone levels are regulated through specialized enzymes, participating not only in their biosynthesis but also in post-signaling processes for signal inactivation and cue depletion. Arabidopsis thaliana (At) carboxylesterase 15 (CXE15) and carboxylesterase 20 (CXE20) have been shown to deplete strigolactones (SLs) that coordinate various growth and developmental processes and function as signaling molecules in the rhizosphere. Here, we elucidate the X-ray crystal structures of AtCXE15 (both apo and SL intermediate bound) and AtCXE20, revealing insights into the mechanisms of SL binding and catabolism. The N-terminal regions of CXE15 and CXE20 exhibit distinct secondary structures, with CXE15 characterized by an alpha helix and CXE20 by an alpha/beta fold. These structural differences play pivotal roles in regulating variable SL hydrolysis rates. Our findings, both in vitro and in planta, indicate that a transition of the N-terminal helix domain of CXE15 between open and closed forms facilitates robust SL hydrolysis. The results not only illuminate the distinctive process of phytohormone breakdown but also uncover a molecular architecture and mode of plasticity within a specific class of carboxylesterases.

PubMed: 39090154
DOI: 10.1038/s41467-024-50928-3

実験手法

X-RAY DIFFRACTION (2.3 Å)