ArticleNature plants2023
Structural and biochemical insight into a modular β-1,4-galactan synthase in plants.
Article in Nature plants, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- Loss of galactan synthesis in pea (Pisum sativum) causes defects in organ expansion and is associated with increased extensin content.Plant molecular biology · 2026Article
- Structural basis of chondroitin sulfate backbone polymer synthesis.Nature communications · 2026Article
- A characterization of recombinant Arabidopsis FRIABLE1 (FRB1) reveals robust rhamnogalacturonan-I rhamnosyltransferase activity and critical catalytic residues.The Journal of biological chemistry · 2026Article
- Detailed Method for the Purification of Rhamnogalacturonan-I (RG-I) inBio-protocol · 2026Article
- Multiprotein Complexes of Plant Glycosyltransferases Involved in Their Function and Trafficking.Plants (Basel, Switzerland) · 2025Review
- The molecular architecture distinctions between compression, opposite and normal wood ofFrontiers in plant science · 2025Article
- The plant cell wall-dynamic, strong, and adaptable-is a natural shapeshifter.The Plant cell · 2024Review
- Enzymes in 3D: Synthesis, remodelling, and hydrolysis of cell wall (1,3;1,4)-β-glucans.Plant physiology · 2023Article
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Authors and funding
14 authors at 4 institutions in 1 country.
Funding
Abstract
Rhamnogalacturonan I (RGI) is a structurally complex pectic polysaccharide with a backbone of alternating rhamnose and galacturonic acid residues substituted with arabinan and galactan side chains. Galactan synthase 1 (GalS1) transfers galactose and arabinose to either extend or cap the β-1,4-galactan side chains of RGI, respectively. Here we report the structure of GalS1 from Populus trichocarpa, showing a modular protein consisting of an N-terminal domain that represents the founding member of a new family of carbohydrate-binding module, CBM95, and a C-terminal glycosyltransferase family 92 (GT92) catalytic domain that adopts a GT-A fold. GalS1 exists as a dimer in vitro, with stem domains interacting across the chains in a 'handshake' orientation that is essential for maintaining stability and activity. In addition to understanding the enzymatic mechanism of GalS1, we gained insight into the donor and acceptor substrate binding sites using deep evolutionary analysis, molecular simulations and biochemical studies. Combining all the results, a mechanism for GalS1 catalysis and a new model for pectic galactan side-chain addition are proposed.
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Registered trials
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.