7UPV

Structure of maize BZR1-type beta-amylase provides new insights into its noncatalytic adaptation

7UPV の概要

• エントリーDOI: 10.2210/pdb7upv/pdb
• 分子名称: Beta-amylase, GLYCEROL (3 entities in total)
• 機能のキーワード: gh-14, maize beta-amylase, bzr1-bam8, hydrolase
• 由来する生物種: Zea mays
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51539.96

構造登録者

Palayam, M.,Sun, F.,Shabek, N. (登録日: 2022-04-18, 公開日: 2022-08-17, 最終更新日: 2024-11-06)

主引用文献

Sun, F.,Palayam, M.,Shabek, N.
Structure of maize BZR1-type beta-amylase BAM8 provides new insights into its noncatalytic adaptation.
J.Struct.Biol., 214:107885-107885, 2022

PubMed Abstract: Plant β-amylase (BAM) proteins play an essential role in growth, development, stress response, and hormone regulation. Despite their typical (β/α) barrel structure as active catalysts in starch breakdown, catalytically inactive BAMs are implicated in diverse yet elusive functions in plants. The noncatalytic BAM7/8 contain N-terminal BZR1 domains and were shown to be involved in the regulation of brassinosteroid signaling and possibly serve as sensors of yet an uncharacterized metabolic signal. While the structures of several catalytically active BAMs have been reported, structural characterization of the catalytically inactive BZR1-type BAMs remain unknown. Here, we determine the crystal structure of β-amylase domain of Zea mays BAM8/BES1/BZR1-5 and provide comprehensive insights into its noncatalytic adaptation. Using structural-guided comparison combined with biochemical analysis and molecular dynamics simulations, we revealed conformational changes in multiple distinct highly conserved regions resulting in rearrangement of the binding pocket. Altogether, this study adds a new layer of understanding to starch breakdown mechanism and elucidates the acquired adjustments of noncatalytic BZR1-type BAMs as putative regulatory domains and/or metabolic sensors in plants.

PubMed: 35961473
DOI: 10.1016/j.jsb.2022.107885

実験手法

X-RAY DIFFRACTION (1.84 Å)