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Structure of the acrosomal bundle

Author

Listed:
  • Michael F. Schmid

    (Baylor College of Medicine)

  • Michael B. Sherman

    (Baylor College of Medicine
    Purdue University)

  • Paul Matsudaira

    (Whitehead Institute)

  • Wah Chiu

    (Baylor College of Medicine)

Abstract

In the unactivated Limulus sperm, a 60-µm-long bundle of actin filaments crosslinked by the protein scruin is bent and twisted into a coil around the base of the nucleus. At fertilization, the bundle uncoils and fully extends in five seconds to support a finger of membrane known as the acrosomal process. This biological spring is powered by stored elastic energy and does not require the action of motor proteins or actin polymerization1. In a 9.5-Å electron cryomicroscopic structure of the extended bundle, we show that twist, tilt and rotation of actin–scruin subunits deviate widely from a ‘standard’ F-actin filament. This variability in structural organization allows filaments to pack into a highly ordered and rigid bundle in the extended state and suggests a mechanism for storing and releasing energy between coiled and extended states without disassembly.

Suggested Citation

  • Michael F. Schmid & Michael B. Sherman & Paul Matsudaira & Wah Chiu, 2004. "Structure of the acrosomal bundle," Nature, Nature, vol. 431(7004), pages 104-107, September.
    • Handle: RePEc:nat:nature:v:431:y:2004:i:7004:d:10.1038_nature02881
    DOI: 10.1038/nature02881
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    Cited by:

    1. Srinivas Ramachandran & Adrian W R Serohijos & Le Xu & Gerhard Meissner & Nikolay V Dokholyan, 2009. "A Structural Model of the Pore-Forming Region of the Skeletal Muscle Ryanodine Receptor (RyR1)," PLOS Computational Biology, Public Library of Science, vol. 5(4), pages 1-10, April.

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