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Science 17 December 1993:
Vol. 262. no. 5141, pp. 1864 - 1867
DOI: 10.1126/science.8266073
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Articles

Science, Vol 262, Issue 5141, 1864-1867
Copyright © 1993 by American Association for the Advancement of Science

articles

The crystal structure of lysin, a fertilization protein

A Shaw, DE McRee, VD Vacquier, and CD Stout

Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037-1093.

Lysin, a protein from abalone sperm, creates a hole in the envelope of the egg, permitting the sperm to pass through the envelope and fuse with the egg. The structure of lysin, refined at 1.9 angstroms resolution, reveals an alpha-helical, amphipathic molecule. The surface of the protein exhibits three features: two tracks of basic residues that span the length of the molecule, a solvent-exposed cluster of aromatic and aliphatic amino acids, and an extended amino-terminal hypervariable domain that is species-specific. The structure suggests possible mechanisms of action.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Positive Selection on an Acrosomal Sperm Protein, M7 Lysin, in Three Species of the Mussel Genus Mytilus.
C. Riginos and J. H. McDonald (2003)
Mol. Biol. Evol. 20, 200-207
   Abstract »    Full Text »    PDF »
All males are not created equal: Fertility differences depend on gamete recognition polymorphisms in sea urchins.
S. R. Palumbi (1999)
PNAS 96, 12632-12637
   Abstract »    Full Text »    PDF »
Evolution of Gamete Recognition Proteins.
V. D. Vacquier (1998)
Science 281, 1995-1998
   Abstract »    Full Text »
Concerted Evolution in an Egg Receptor for a Rapidly Evolving Abalone Sperm Protein.
W. J. Swanson and V. D. Vacquier (1998)
Science 281, 710-712
   Abstract »    Full Text »
The abalone egg vitelline envelope receptor for sperm lysin is a giant multivalent molecule.
W. J. Swanson and V. D. Vacquier (1997)
PNAS 94, 6724-6729
   Abstract »    Full Text »    PDF »


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