8ZGE

Human lysine O-link glycosylation complex, LH3/ColGalT1 tetramer with bound UDP-galactose

8ZGE の概要

• エントリーDOI: 10.2210/pdb8zge/pdb
• EMDBエントリー: 60076
• 分子名称: Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3, Procollagen galactosyltransferase 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• 機能のキーワード: complex, hydroxylase, glycosyltransferase, er protein, cytosolic protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 334721.33

構造登録者

Peng, J.,Li, W.,Yao, D.,Xia, Y.,Wang, Q.,Cai, Y.,Li, S.,Cao, M.,Shen, Y.,Ma, P.,Liao, R.,Qin, A.,Cao, Y. (登録日: 2024-05-09, 公開日: 2025-03-19, 最終更新日: 2025-03-26)

主引用文献

Peng, J.,Li, W.,Yao, D.,Xia, Y.,Wang, Q.,Cai, Y.,Li, S.,Cao, M.,Shen, Y.,Ma, P.,Liao, R.,Zhao, J.,Qin, A.,Cao, Y.
The structural basis for the human procollagen lysine hydroxylation and dual-glycosylation.
Nat Commun, 16:2436-2436, 2025

PubMed Abstract: The proper assembly and maturation of collagens necessitate the orchestrated hydroxylation and glycosylation of multiple lysyl residues in procollagen chains. Dysfunctions in this multistep modification process can lead to severe collagen-associated diseases. To elucidate the coordination of lysyl processing activities, we determine the cryo-EM structures of the enzyme complex formed by LH3/PLOD3 and GLT25D1/ColGalT1, designated as the KOGG complex. Our structural analysis reveals a tetrameric complex comprising dimeric LH3/PLOD3s and GLT25D1/ColGalT1s, assembled with interactions involving the N-terminal loop of GLT25D1/ColGalT1 bridging another GLT25D1/ColGalT1 and LH3/PLOD3. We further elucidate the spatial configuration of the hydroxylase, galactosyltransferase, and glucosyltransferase sites within the KOGG complex, along with the key residues involved in substrate binding at these enzymatic sites. Intriguingly, we identify a high-order oligomeric pattern characterized by the formation of a fiber-like KOGG polymer assembled through the repetitive incorporation of KOGG tetramers as the biological unit.

PubMed: 40069201
DOI: 10.1038/s41467-025-57768-9

実験手法

ELECTRON MICROSCOPY (3.4 Å)