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Crystal-structure and subunit dynamics of the abalone sperm lysin dimer - egg envelopes dissociate dimers, the monomer is the active species

Academic Article
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Overview

authors

  • Shaw, A.
  • Fortes, P. A. G.
  • Stout, C. David
  • Vacquier, V. D.

publication date

  • September 1995

journal

  • Journal of Cell Biology  Journal

abstract

  • Lysin is a 16-kD acrosomal protein used by abalone spermatozoa to create a hole in the egg vitelline envelope (VE) by a nonenzymatic mechanism. The crystal structure of the lysin monomer is known at 1.9 A resolution. The surface of the molecule reveals two tracks of basic residues running the length of one surface of the molecule and a patch of solvent-exposed hydrophobic residues on the opposite surface. Here we report that lysin dimerizes via interaction of the hydrophobic patches of monomers. Triton X-100 dissociates the dimer. The crystal structure of the dimer is described at 2.75 A resolution. Fluorescence energy transfer experiments show that the dimer has an approximate KD of 1 microM and that monomers exchange rapidly between dimers. Addition of isolated egg VE dissociates dimers, implicating monomers as the active species in the dissolution reaction. This work represents the first step in the elucidation of the mechanism by which lysin enables abalone spermatozoa to create a hole in the egg envelope during fertilization.

subject areas

  • Animals
  • Crystallization
  • Egg Proteins
  • Female
  • Fertilization
  • Fluorescent Dyes
  • Male
  • Mollusca
  • Mucoproteins
  • Protein Binding
  • Spermatozoa
  • Vitelline Membrane
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Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.130.5.1117

PubMed ID

  • 7657696
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Additional Document Info

start page

  • 1117

end page

  • 1125

volume

  • 130

issue

  • 5

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