Structure of the acrosomal bundle
Michael F. Schmid,
Michael B. Sherman,
Paul Matsudaira and
Wah Chiu ()
Additional contact information
Michael F. Schmid: Baylor College of Medicine
Michael B. Sherman: Baylor College of Medicine
Paul Matsudaira: Whitehead Institute
Wah Chiu: Baylor College of Medicine
Nature, 2004, vol. 431, issue 7004, 104-107
Abstract:
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.
Date: 2004
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Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:431:y:2004:i:7004:d:10.1038_nature02881
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DOI: 10.1038/nature02881
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