Evidence map›Paper›PMID 37572661›Full record

ArticleStructure (London, England : 1993)2023

Insights into substrate coordination and glycosyl transfer of poplar cellulose synthase-8.

Preeti Verma, Albert L Kwansa, Ruoya Ho, Yaroslava G Yingling, Jochen Zimmer

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.4field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 13 citations in OpenAlex.

  1. A molecular description of plant cellulose biosynthesis inhibition.bioRxiv : the preprint server for biology · 2026
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Preeti VermaDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22903, USA.
Albert L KwansaDepartment of Materials Science and Engineering, North Carolina State University, Raleigh, NC 27695, USA.
Ruoya HoDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22903, USA; Howard Hughes Medical Institute, University of Virginia, Charlottesville, VA 22903, USA.
Yaroslava G YinglingDepartment of Materials Science and Engineering, North Carolina State University, Raleigh, NC 27695, USA.
Jochen ZimmerDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22903, USA; Howard Hughes Medical Institute, University of Virginia, Charlottesville, VA 22903, USA. Electronic address: jz3x@virginia.edu.
Howard Hughes Medical Institute · USNorth Carolina State University · USUniversity of Virginia · US

Funding

Synthesis, secretion and assembly of extracellular complex carbohydrates in Gram-negative bacteriaR35GM144130 · NIGMS · UNIVERSITY OF VIRGINIA · PI Jochen Zimmer · 2022 to 2026
$2.5M
Howard Hughes Medical InstituteNIGMS NIH HHS R35 GM144130
6 · The paper itself

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.

Indexed as

CelluloseGlucosyltransferasesGlucoseUridine DiphosphateCellulosecellulose synthaseGlucoseGlucosyltransferasesUridine Diphosphatecellulose biosynthesiscryo-electron microscopyglycosyltransferasemolecular dynamics simulationsmutagenesis

Identifiers

PMID37572661
PMCPMC10592267
OpenAlexW4385760662

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.