3lyn: Difference between revisions
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{{STRUCTURE_3lyn| PDB=3lyn | SCENE= }} | |||
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'''STRUCTURE OF GREEN ABALONE LYSIN DIMER''' | '''STRUCTURE OF GREEN ABALONE LYSIN DIMER''' | ||
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[[Category: Stout, C D.]] | [[Category: Stout, C D.]] | ||
[[Category: Vacquier, V D.]] | [[Category: Vacquier, V D.]] | ||
[[Category: | [[Category: Abalone lysin]] | ||
[[Category: | [[Category: Fertilization protein]] | ||
[[Category: | [[Category: Gamete recognition protein]] | ||
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Revision as of 19:06, 4 May 2008
STRUCTURE OF GREEN ABALONE LYSIN DIMER
Overview
Abalone sperm lysin is a 16 kDa acrosomal protein used by sperm to create a hole in the egg vitelline envelope. Lysins from seven California abalone exhibit species-specificity in binding to their egg receptor, and range in sequence identity from 63 % to 90 %. The crystal structure of the sperm lysin dimer from Haliotis fulgens (green abalone) has been determined to 1.71 A by multiple isomorphous replacement. Comparisons with the structure of the lysin dimer from Haliotis rufescens (red abalone) reveal a similar overall fold and conservation of features contributing to lysin's amphipathic character. The two structures do, however, exhibit differences in surface residues and electrostatics. A large clustering of non-conserved surface residues around the waist and clefts of the dimer, and differences in charged residues around these regions, indicate areas of the molecule which may be involved in species-specific egg recognition.
About this Structure
3LYN is a Single protein structure of sequence from Haliotis fulgens. Full crystallographic information is available from OCA.
Reference
The high resolution crystal structure of green abalone sperm lysin: implications for species-specific binding of the egg receptor., Kresge N, Vacquier VD, Stout CD, J Mol Biol. 2000 Mar 10;296(5):1225-34. PMID:10698629 Page seeded by OCA on Sun May 4 22:06:17 2008
