8G27

Hybrid aspen cellulose synthase-8 bound to UDP

8G27 の概要

• エントリーDOI: 10.2210/pdb8g27/pdb
• 関連するPDBエントリー: 6WLB
• EMDBエントリー: 29678
• 関連するBIRD辞書のPRD_ID: PRD_900005
• 分子名称: Cellulose synthase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, URIDINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: cellulose, cell wall, udp, plant protein, transferase
• 由来する生物種: Populus tremula x Populus tremuloides
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 339688.44

構造登録者

Verma, P.,Zimmer, J. (登録日: 2023-02-03, 公開日: 2023-03-01, 最終更新日: 2025-06-04)

主引用文献

Verma, P.,Kwansa, A.L.,Ho, R.,Yingling, Y.G.,Zimmer, J.
Insights into substrate coordination and glycosyl transfer of poplar cellulose synthase-8.
Biorxiv, 2023

PubMed Abstract: Cellulose is an abundant cell wall component of land plants. It is synthesized from UDP-activated glucose molecules by cellulose synthase, a membrane-integrated processive glycosyltransferase. Cellulose synthase couples the elongation of the cellulose polymer with its translocation across the plasma membrane. Here, we present substrate and product-bound cryogenic electron microscopy structures of the homotrimeric cellulose synthase isoform-8 (CesA8) from hybrid aspen (poplar). UDP-glucose binds to a conserved catalytic pocket adjacent to the entrance to a transmembrane channel. The substrate's glucosyl unit is coordinated by conserved residues of the glycosyltransferase domain and amphipathic interface helices. Site-directed mutagenesis of a conserved gating loop capping the active site reveals its critical function for catalytic activity. Molecular dynamics simulations reveal prolonged interactions of the gating loop with the substrate molecule, particularly across its central conserved region. These transient interactions likely facilitate the proper positioning of the substrate molecule for glycosyl transfer and cellulose translocation.

PubMed: 36798277
DOI: 10.1101/2023.02.07.527505

実験手法

ELECTRON MICROSCOPY (3.3 Å)