IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v539y2016i7627d10.1038_nature19825.html
   My bibliography  Save this article

De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure

Author

Listed:
  • Jacques-Philippe Colletier

    (Institut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CEA, CNRS)

  • Michael R. Sawaya

    (UCLA-DOE Institute for Genomics and Proteomics, University of California
    Howard Hughes Medical Institute, University of California)

  • Mari Gingery

    (UCLA-DOE Institute for Genomics and Proteomics, University of California)

  • Jose A. Rodriguez

    (UCLA-DOE Institute for Genomics and Proteomics, University of California)

  • Duilio Cascio

    (UCLA-DOE Institute for Genomics and Proteomics, University of California)

  • Aaron S. Brewster

    (Lawrence Berkeley National Laboratory)

  • Tara Michels-Clark

    (Lawrence Berkeley National Laboratory)

  • Robert H. Hice

    (Molecular and Developmental Biology, University of California)

  • Nicolas Coquelle

    (Institut de Biologie Structurale (IBS), Univ. Grenoble Alpes, CEA, CNRS)

  • Sébastien Boutet

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • Garth J. Williams

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • Marc Messerschmidt

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • Daniel P. DePonte

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • Raymond G. Sierra

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • Hartawan Laksmono

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • Jason E. Koglin

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • Mark S. Hunter

    (Linac Coherent Light Source, SLAC National Accelerator Laboratory)

  • Hyun-Woo Park

    (Molecular and Developmental Biology, University of California
    California Baptist University)

  • Monarin Uervirojnangkoorn

    (Molecular and Cellular Physiology, and Howard Hughes Medical Institute, Stanford University)

  • Dennis K. Bideshi

    (Molecular and Developmental Biology, University of California
    California Baptist University)

  • Axel T. Brunger

    (Molecular and Cellular Physiology, and Howard Hughes Medical Institute, Stanford University)

  • Brian A. Federici

    (Molecular and Developmental Biology, University of California)

  • Nicholas K. Sauter

    (Lawrence Berkeley National Laboratory)

  • David S. Eisenberg

    (UCLA-DOE Institute for Genomics and Proteomics, University of California
    Howard Hughes Medical Institute, University of California)

Abstract

BinAB is a naturally occurring paracrystalline larvicide distributed worldwide to combat the devastating diseases borne by mosquitoes. These crystals are composed of homologous molecules, BinA and BinB, which play distinct roles in the multi-step intoxication process, transforming from harmless, robust crystals, to soluble protoxin heterodimers, to internalized mature toxin, and finally to toxic oligomeric pores. The small size of the crystals—50 unit cells per edge, on average—has impeded structural characterization by conventional means. Here we report the structure of Lysinibacillus sphaericus BinAB solved de novo by serial-femtosecond crystallography at an X-ray free-electron laser. The structure reveals tyrosine- and carboxylate-mediated contacts acting as pH switches to release soluble protoxin in the alkaline larval midgut. An enormous heterodimeric interface appears to be responsible for anchoring BinA to receptor-bound BinB for co-internalization. Remarkably, this interface is largely composed of propeptides, suggesting that proteolytic maturation would trigger dissociation of the heterodimer and progression to pore formation.

Suggested Citation

  • Jacques-Philippe Colletier & Michael R. Sawaya & Mari Gingery & Jose A. Rodriguez & Duilio Cascio & Aaron S. Brewster & Tara Michels-Clark & Robert H. Hice & Nicolas Coquelle & Sébastien Boutet & Gart, 2016. "De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure," Nature, Nature, vol. 539(7627), pages 43-47, November.
    • Handle: RePEc:nat:nature:v:539:y:2016:i:7627:d:10.1038_nature19825
    DOI: 10.1038/nature19825
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature19825
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature19825?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
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

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


    Cited by:

    1. Guillaume Tetreau & Michael R. Sawaya & Elke Zitter & Elena A. Andreeva & Anne-Sophie Banneville & Natalie A. Schibrowsky & Nicolas Coquelle & Aaron S. Brewster & Marie Luise Grünbein & Gabriela Nass , 2022. "De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    2. Robert Schönherr & Juliane Boger & J. Mia Lahey-Rudolph & Mareike Harms & Jacqueline Kaiser & Sophie Nachtschatt & Marla Wobbe & Rainer Duden & Peter König & Gleb Bourenkov & Thomas R. Schneider & Lar, 2024. "A streamlined approach to structure elucidation using in cellulo crystallized recombinant proteins, InCellCryst," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    3. Izumi Ishigami & Raymond G. Sierra & Zhen Su & Ariana Peck & Cong Wang & Frederic Poitevin & Stella Lisova & Brandon Hayes & Frank R. Moss & Sébastien Boutet & Robert E. Sublett & Chun Hong Yoon & Syu, 2023. "Structural insights into functional properties of the oxidized form of cytochrome c oxidase," Nature Communications, Nature, vol. 14(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:nature:v:539:y:2016:i:7627:d:10.1038_nature19825. 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.