ArticleNature communications2022
The structure of EXTL3 helps to explain the different roles of bi-domain exostosins in heparan sulfate synthesis.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 34 citations in OpenAlex.
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- XYLAN O-ACETYLTRANSFERASE 6 promotes xylan synthesis by forming a complex with IRX10 and governs wall formation in rice.The Plant cell · 2024Article
- Restoring protein glycosylation with GlycoShape.Nature methods · 2024Article
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- Chemo-enzymatic synthesis of tetrasaccharide linker peptides to study the divergent step in glycosaminoglycan biosynthesis.Glycobiology · 2024Article
- Structural and mechanistic characterization of bifunctional heparan sulfate N-deacetylase-N-sulfotransferase 1.Nature communications · 2024Article
- AEG-1 as a Novel Therapeutic Target in Colon Cancer: A Study from Silencing AEG-1 in BALB/c Mice to Large Data Analysis.Current gene therapy · 2024Article
- The biosynthesis, degradation, and function of cell wall β-xylosylated xyloglucan mirrors that of arabinoxyloglucan.The New phytologist · 2023Article
- Molecular mechanism of decision-making in glycosaminoglycan biosynthesis.Nature communications · 2023Article
- Structural basis for heparan sulfate co-polymerase action by the EXT1-2 complex.Nature chemical biology · 2023Article
- DALI shines a light on remote homologs: One hundred discoveries.Protein science : a publication of the Protein Society · 2023Article
- Structure of the human heparan sulfate polymerase complex EXT1-EXT2.Nature communications · 2022Article
- β-1,4-Xylan backbone synthesis in higher plants: How complex can it be?Frontiers in plant science · 2022Article
- Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2021-2022.Mass spectrometry reviewsReview
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Authors and funding
11 authors at 4 institutions in 4 countries.
Funding
Abstract
Heparan sulfate is a highly modified O-linked glycan that performs diverse physiological roles in animal tissues. Though quickly modified, it is initially synthesised as a polysaccharide of alternating β-D-glucuronosyl and N-acetyl-α-D-glucosaminyl residues by exostosins. These enzymes generally possess two glycosyltransferase domains (GT47 and GT64)-each thought to add one type of monosaccharide unit to the backbone. Although previous structures of murine exostosin-like 2 (EXTL2) provide insight into the GT64 domain, the rest of the bi-domain architecture is yet to be characterised; hence, how the two domains co-operate is unknown. Here, we report the structure of human exostosin-like 3 (EXTL3) in apo and UDP-bound forms. We explain the ineffectiveness of EXTL3's GT47 domain to transfer β-D-glucuronosyl units, and we observe that, in general, the bi-domain architecture would preclude a processive mechanism of backbone extension. We therefore propose that heparan sulfate backbone polymerisation occurs by a simple dissociative mechanism.
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