3lyn
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(New page: 200px<br /><applet load="3lyn" size="450" color="white" frame="true" align="right" spinBox="true" caption="3lyn, resolution 1.70Å" /> '''STRUCTURE OF GREEN A...)
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Revision as of 17:42, 20 November 2007
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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
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