IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v11y2020i1d10.1038_s41467-020-14833-9.html
   My bibliography  Save this article

The structural basis of fungal glucuronoyl esterase activity on natural substrates

Author

Listed:
  • Heidi A. Ernst

    (University of Copenhagen, Universitetsparken 5)

  • Caroline Mosbech

    (Technical University of Denmark)

  • Annette E. Langkilde

    (University of Copenhagen, Universitetsparken 2)

  • Peter Westh

    (Technical University of Denmark)

  • Anne S. Meyer

    (Technical University of Denmark)

  • Jane W. Agger

    (Technical University of Denmark)

  • Sine Larsen

    (University of Copenhagen, Universitetsparken 5)

Abstract

Structural and functional studies were conducted of the glucuronoyl esterase (GE) from Cerrena unicolor (CuGE), an enzyme catalyzing cleavage of lignin-carbohydrate ester bonds. CuGE is an α/β-hydrolase belonging to carbohydrate esterase family 15 (CE15). The enzyme is modular, comprised of a catalytic and a carbohydrate-binding domain. SAXS data show CuGE as an elongated rigid molecule where the two domains are connected by a rigid linker. Detailed structural information of the catalytic domain in its apo- and inactivated form and complexes with aldouronic acids reveal well-defined binding of the 4-O-methyl-a-D-glucuronoyl moiety, not influenced by the nature of the attached xylo-oligosaccharide. Structural and sequence comparisons within CE15 enzymes reveal two distinct structural subgroups. CuGE belongs to the group of fungal CE15-B enzymes with an open and flat substrate-binding site. The interactions between CuGE and its natural substrates are explained and rationalized by the structural results, microscale thermophoresis and isothermal calorimetry.

Suggested Citation

  • Heidi A. Ernst & Caroline Mosbech & Annette E. Langkilde & Peter Westh & Anne S. Meyer & Jane W. Agger & Sine Larsen, 2020. "The structural basis of fungal glucuronoyl esterase activity on natural substrates," Nature Communications, Nature, vol. 11(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14833-9
    DOI: 10.1038/s41467-020-14833-9
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-020-14833-9
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-020-14833-9?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
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Zhiyou Zong & Scott Mazurkewich & Caroline S. Pereira & Haohao Fu & Wensheng Cai & Xueguang Shao & Munir S. Skaf & Johan Larsbrink & Leila Lo Leggio, 2022. "Mechanism and biomass association of glucuronoyl esterase: an α/β hydrolase with potential in biomass conversion," Nature Communications, Nature, vol. 13(1), pages 1-10, 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:11:y:2020:i:1:d:10.1038_s41467-020-14833-9. 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.

    We have no bibliographic references for this item. You can help adding them by using 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.