7SP9
Chlorella virus Hyaluronan Synthase in the GlcNAc-primed channel-closed state
Summary for 7SP9
| Entry DOI | 10.2210/pdb7sp9/pdb |
| EMDB information | 25369 |
| Descriptor | Nanobody 872, Nanobody 881, Hyaluronan synthase, ... (5 entities in total) |
| Functional Keywords | glycosyltransferase, hyaluronan, membrane protein |
| Biological source | Lama glama More |
| Total number of polymer chains | 3 |
| Total formula weight | 96093.42 |
| Authors | Maloney, F.P.,Kuklewicz, J.,Zimmer, J. (deposition date: 2021-11-02, release date: 2022-04-06, Last modification date: 2022-04-20) |
| Primary citation | Maloney, F.P.,Kuklewicz, J.,Corey, R.A.,Bi, Y.,Ho, R.,Mateusiak, L.,Pardon, E.,Steyaert, J.,Stansfeld, P.J.,Zimmer, J. Structure, substrate recognition and initiation of hyaluronan synthase. Nature, 604:195-201, 2022 Cited by PubMed Abstract: Hyaluronan is an acidic heteropolysaccharide comprising alternating N-acetylglucosamine and glucuronic acid sugars that is ubiquitously expressed in the vertebrate extracellular matrix. The high-molecular-mass polymer modulates essential physiological processes in health and disease, including cell differentiation, tissue homeostasis and angiogenesis. 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. 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. PubMed: 35355017DOI: 10.1038/s41586-022-04534-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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