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8G2J

Hybrid aspen cellulose synthase-8 bound to UDP-glucose

Summary for 8G2J
Entry DOI10.2210/pdb8g2j/pdb
EMDB information29679
Related PRD IDPRD_900016
DescriptorCellulose synthase, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, URIDINE-5'-DIPHOSPHATE-GLUCOSE, ... (4 entities in total)
Functional Keywordscellulose, cell wall, udp, plant protein
Biological sourcePopulus tremula x P. tremuloides/Amanita muscaria mixed EST library
Total number of polymer chains3
Total formula weight341707.05
Authors
Verma, P.,Zimmer, J. (deposition date: 2023-02-04, release date: 2023-03-01, Last modification date: 2025-05-14)
Primary citationVerma, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

243531

数据于2025-10-22公开中

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