8SNE

Chlorella virus Hyaluronan Synthase bound to GlcA extended GlcNAc primer and UDP

8SNE の概要

• エントリーDOI: 10.2210/pdb8sne/pdb
• EMDBエントリー: 40624
• 分子名称: Hyaluronan synthase, Nanobody 872, Nanobody 886, ... (8 entities in total)
• 機能のキーワード: hyaluronic acid, hyaluronan, ha, has, glycosyltransferase, gt, membrane protein, nanobody, n-acetylglucosamine, glucuronic acid, transferase
• 由来する生物種: Paramecium bursaria Chlorella virus CZ-2; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 97556.74

構造登録者

Stephens, Z.,Zimmer, J. (登録日: 2023-04-27, 公開日: 2024-05-01, 最終更新日: 2025-02-05)

主引用文献

Gorniak, I.,Stephens, Z.,Erramilli, S.K.,Gawda, T.,Kossiakoff, A.A.,Zimmer, J.
Structural insights into translocation and tailored synthesis of hyaluronan.
Nat.Struct.Mol.Biol., 32:161-171, 2025

PubMed Abstract: Hyaluronan (HA) is an essential component of the vertebrate extracellular matrix. It is a heteropolysaccharide of N-acetylglucosamine (GlcNAc) and glucuronic acid (GlcA) reaching several megadaltons in healthy tissues. HA is synthesized and translocated in a coupled reaction by HA synthase (HAS). Here, structural snapshots of HAS provide insights into HA biosynthesis, from substrate recognition to HA elongation and translocation. We monitor the extension of a GlcNAc primer with GlcA, reveal the coordination of the uridine diphosphate product by a conserved gating loop and capture the opening of a translocation channel to coordinate a translocating HA polymer. Furthermore, we identify channel-lining residues that modulate HA product lengths. Integrating structural and biochemical analyses suggests an avenue for polysaccharide engineering based on finely tuned enzymatic activity and HA coordination.

PubMed: 39322765
DOI: 10.1038/s41594-024-01389-1

実験手法

ELECTRON MICROSCOPY (3 Å)