IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v15y2024i1d10.1038_s41467-024-52321-6.html
   My bibliography  Save this article

The structural basis for the collagen processing by human P3H1/CRTAP/PPIB ternary complex

Author

Listed:
  • Wenguo Li

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

  • Junjiang Peng

    (Shanghai Jiao Tong University School of Medicine)

  • Deqiang Yao

    (Shanghai Jiao Tong University School of Medicine)

  • Bing Rao

    (Shanghai Jiao Tong University School of Medicine
    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)

  • 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)

  • An Qin

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

  • Jie Zhao

    (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

Collagen posttranslational processing is crucial for its proper assembly and function. Disruption of collagen processing leads to tissue development and structure disorders like osteogenesis imperfecta (OI). OI-related collagen processing machinery includes prolyl 3-hydroxylase 1 (P3H1), peptidyl-prolyl cis-trans isomerase B (PPIB), and cartilage-associated protein (CRTAP), with their structural organization and mechanism unclear. We determine cryo-EM structures of the P3H1/CRTAP/PPIB complex. The active sites of P3H1 and PPIB form a face-to-face bifunctional reaction center, indicating a coupled modification mechanism. The structure of the P3H1/CRTAP/PPIB/collagen peptide complex reveals multiple binding sites, suggesting a substrate interacting zone. Unexpectedly, a dual-ternary complex is observed, and the balance between ternary and dual-ternary states can be altered by mutations in the P3H1/PPIB active site and the addition of PPIB inhibitors. These findings provide insights into the structural basis of collagen processing by P3H1/CRTAP/PPIB and the molecular pathology of collagen-related disorders.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-52321-6
    DOI: 10.1038/s41467-024-52321-6
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-024-52321-6
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-024-52321-6?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    References listed on IDEAS

    as
    1. Rasheduzzaman Chowdhury & Ivanhoe K. H. Leung & Ya-Min Tian & Martine I. Abboud & Wei Ge & Carmen Domene & François-Xavier Cantrelle & Isabelle Landrieu & Adam P. Hardy & Christopher W. Pugh & Peter J, 2016. "Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases," Nature Communications, Nature, vol. 7(1), pages 1-10, November.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Tianshi Feng & Xuemei Zhao & Ping Gu & Wah Yang & Cunchuan Wang & Qingyu Guo & Qiaoyun Long & Qing Liu & Ying Cheng & Jin Li & Cynthia Kwan Yui Cheung & Donghai Wu & Xinyu Kong & Yong Xu & Dewei Ye & , 2022. "Adipocyte-derived lactate is a signalling metabolite that potentiates adipose macrophage inflammation via targeting PHD2," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-52321-6. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.