Ontology highlight
ABSTRACT:
SUBMITTER: Shaw A
PROVIDER: S-EPMC2120550 | biostudies-other | 1995 Sep
REPOSITORIES: biostudies-other
Shaw A A Fortes P A PA Stout C D CD Vacquier V D VD
The Journal of cell biology 19950901 5
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. ...[more]