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TitleStructure of the acrosomal bundle.
Journal, issue, pagesNature, Vol. 431, Issue 7004, Page 104-107, Year 2004
Publish dateSep 2, 2004
AuthorsMichael F Schmid / Michael B Sherman / Paul Matsudaira / Wah Chiu /
PubMed AbstractIn the unactivated Limulus sperm, a 60- micro m-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 ...In the unactivated Limulus sperm, a 60- micro m-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 polymerization. In a 9.5-A 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.
External linksNature / PubMed:15343340
MethodsEM (helical sym.)
Resolution9.5 Å
Structure data

EMDB-1088:
Structure of the acrosomal bundle.
Method: EM (helical sym.) / Resolution: 9.5 Å

Source
  • Limulus polyphemus (Atlantic horseshoe crab)

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