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TitleStructure, substrate recognition and initiation of hyaluronan synthase.
Journal, issue, pagesNature, Vol. 604, Issue 7904, Page 195-201, Year 2022
Publish dateMar 30, 2022
AuthorsFinn P Maloney / Jeremi Kuklewicz / Robin A Corey / Yunchen Bi / Ruoya Ho / Lukasz Mateusiak / Els Pardon / Jan Steyaert / Phillip J Stansfeld / Jochen Zimmer /
PubMed AbstractHyaluronan is an acidic heteropolysaccharide comprising alternating N-acetylglucosamine and glucuronic acid sugars that is ubiquitously expressed in the vertebrate extracellular matrix. The high- ...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.
External linksNature / PubMed:35355017 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.1 Å
Structure data

25366

7sp6

EMDB-25366, PDB-7sp6:
Chlorella virus hyaluronan synthase
Method: EM (single particle) / Resolution: 3.1 Å

25367

7sp7

EMDB-25367, PDB-7sp7:
Chlorella virus hyaluronan synthase inhibited by UDP
Method: EM (single particle) / Resolution: 3.1 Å

25368

7sp8

EMDB-25368, PDB-7sp8:
Chlorella virus Hyaluronan Synthase bound to UDP-GlcNAc
Method: EM (single particle) / Resolution: 2.7 Å

25369

7sp9

EMDB-25369, PDB-7sp9:
Chlorella virus Hyaluronan Synthase in the GlcNAc-primed channel-closed state
Method: EM (single particle) / Resolution: 2.9 Å

25370

7spa

EMDB-25370, PDB-7spa:
Chlorella virus Hyaluronan Synthase in the GlcNAc-primed, channel-open state
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-MN:
Unknown entry

ChemComp-3PE:
1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipid*YM / Phosphatidylethanolamine

ChemComp-UDP:
URIDINE-5'-DIPHOSPHATE / UDP*YM / Uridine diphosphate

ChemComp-UD1:
URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • paramecium bursaria chlorella virus cz-2
  • lama glama (llama)
KeywordsMEMBRANE PROTEIN / glycosyltransferase / hyaluronan

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