The high resolution crystal structure of green abalone sperm lysin: implications for species-specific binding of the egg receptor.
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.
Kresge
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Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037-1093, USA.
Vacquier
V D
VD
Stout
C D
CD
D000177:Acrosome / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017124:Conserved Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D008297:Male; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008974:Mollusca / Q000737:chemistry*; D009088:Mucoproteins / Q000737:chemistry* / Q000378:metabolism*; D010063:Ovum / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D016415:Sequence Alignment; D013045:Species Specificity; D055672:Static Electricity
D009088:Mucoproteins; D011506:Proteins; D011956:Receptors, Cell Surface; C010393:lysin, gastropoda