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

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Listed:
  • Junjiang Peng

    (Shanghai Jiao Tong University School of Medicine
    Shanghai Jiao Tong University School of Medicine)

  • Wenguo Li

    (Shanghai Jiao Tong University School of Medicine
    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
    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
    Shanghai Jiao Tong University School of Medicine)

  • An Qin

    (Shanghai Jiao Tong University School of Medicine
    Shanghai Jiao Tong University School of Medicine)

  • Yu Cao

    (Shanghai Jiao Tong University School of Medicine
    Shanghai Jiao Tong University School of Medicine)

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.

Suggested Citation

  • 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 & Yu Cao, 2025. "The structural basis for the human procollagen lysine hydroxylation and dual-glycosylation," Nature Communications, Nature, vol. 16(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-57768-9
    DOI: 10.1038/s41467-025-57768-9
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    References listed on IDEAS

    as
    1. Wenguo Li & Junjiang Peng & Deqiang Yao & Bing Rao & Ying Xia & Qian Wang & Shaobai Li & Mi Cao & Yafeng Shen & Peixiang Ma & Rijing Liao & An Qin & Jie Zhao & Yu Cao, 2024. "The structural basis for the collagen processing by human P3H1/CRTAP/PPIB ternary complex," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
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    Cited by:

    1. Matteo De Marco & Sristi Raj Rai & Luigi Scietti & Daiana Mattoteia & Stefano Liberi & Elisabetta Moroni & Alberta Pinnola & Alice Vetrano & Claudio Iacobucci & Carlo Santambrogio & Giorgio Colombo & , 2025. "Molecular structure and enzymatic mechanism of the human collagen hydroxylysine galactosyltransferase GLT25D1/COLGALT1," Nature Communications, Nature, vol. 16(1), pages 1-17, December.

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