7sp8

Chlorella virus Hyaluronan Synthase bound to UDP-GlcNAc

spinqualitylabelsall models 7sp8, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7sp8 is a 3 chain structure with sequence from Lama glama and Paramecium bursaria Chlorella virus CZ-2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.7Å Ligands: 3PE, MN, UD1, Y01 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M1H2Q1_9PHYC Publication Abstract from PubMed Hyaluronan is an acidic heteropolysaccharide comprising alternating N-acetylglucosamine and glucuronic acid sugars that is ubiquitously expressed in the vertebrate extracellular matrix(1). The high-molecular-mass polymer modulates essential physiological processes in health and disease, including cell differentiation, tissue homeostasis and angiogenesis(2). Hyaluronan is synthesized by a membrane-embedded processive glycosyltransferase, hyaluronan synthase (HAS), which catalyses the synthesis and membrane translocation of hyaluronan from uridine diphosphate-activated precursors(3,4). Here we describe five cryo-electron microscopy structures of a viral HAS homologue at different states during substrate binding and initiation of polymer synthesis. Combined with biochemical analyses and molecular dynamics simulations, our data reveal how HAS selects its substrates, hydrolyses the first substrate to prime the synthesis reaction, opens a hyaluronan-conducting transmembrane channel, ensures alternating substrate polymerization and coordinates hyaluronan inside its transmembrane pore. Our research suggests a detailed model for the formation of an acidic extracellular heteropolysaccharide and provides insights into the biosynthesis of one of the most abundant and essential glycosaminoglycans in the human body. Structure, substrate recognition and initiation of hyaluronan synthase.,Maloney FP, Kuklewicz J, Corey RA, Bi Y, Ho R, Mateusiak L, Pardon E, Steyaert J, Stansfeld PJ, Zimmer J Nature. 2022 Apr;604(7904):195-201. doi: 10.1038/s41586-022-04534-2. Epub 2022 , Mar 30. PMID:35355017 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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