The structural basis for the human procollagen lysine hydroxylation and dual-glycosylation

Junjiang Peng, Wenguo Li, Deqiang Yao, Ying Xia, Qian Wang, Yan Cai, Shaobai Li, Mi Cao, Yafeng Shen, Peixiang Ma, Rijing Liao, Jie Zhao, An Qin () and Yu Cao ()
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Junjiang Peng: Shanghai Jiao Tong University School of Medicine
Wenguo Li: Shanghai Jiao Tong University School of Medicine
Deqiang Yao: Shanghai Jiao Tong University School of Medicine
Ying Xia: Shanghai Jiao Tong University School of Medicine
Qian Wang: Shanghai Jiao Tong University School of Medicine
Yan Cai: Shanghai Jiao Tong University School of Medicine
Shaobai Li: Shanghai Jiao Tong University School of Medicine
Mi Cao: Shanghai Jiao Tong University School of Medicine
Yafeng Shen: Shanghai Jiao Tong University School of Medicine
Peixiang Ma: Shanghai Jiao Tong University School of Medicine
Rijing Liao: Shanghai Jiao Tong University School of Medicine
Jie Zhao: Shanghai Jiao Tong University School of Medicine
An Qin: Shanghai Jiao Tong University School of Medicine
Yu Cao: Shanghai Jiao Tong University School of Medicine

Nature Communications, 2025, vol. 16, issue 1, 1-13

Abstract: 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.

Date: 2025
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DOI: 10.1038/s41467-025-57768-9

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