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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
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    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. 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.
    3. 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.

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