1lyn
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(New page: 200px<br /><applet load="1lyn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lyn, resolution 2.75Å" /> '''CRYSTAL STRUCTURE AN...)
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Revision as of 18:52, 20 November 2007
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CRYSTAL STRUCTURE AND SUBUNIT DYNAMICS OF THE LYSIN DIMER: EGG ENVELOPES DISSOCIATE DIMERS, THE MONOMER IS THE ACTIVE SPECIES
Overview
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.
About this Structure
1LYN is a Single protein structure of sequence from Haliotis rufescens. Full crystallographic information is available from OCA.
Reference
Crystal structure and subunit dynamics of the abalone sperm lysin dimer: egg envelopes dissociate dimers, the monomer is the active species., Shaw A, Fortes PA, Stout CD, Vacquier VD, J Cell Biol. 1995 Sep;130(5):1117-25. PMID:7657696
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