3LYN

STRUCTURE OF GREEN ABALONE LYSIN DIMER

Summary for 3LYN

• Entry DOI: 10.2210/pdb3lyn/pdb
• Descriptor: SPERM LYSIN (2 entities in total)
• Functional Keywords: abalone lysin, fertilization protein, gamete recognition protein, cell adhesion
• Biological source: Haliotis fulgens
• Cellular location: Cytoplasmic vesicle, secretory vesicle, acrosome lumen : Q01381
• Total number of polymer chains: 2
• Total formula weight: 32692.49

Authors

Kresge, N.,Vacquier, V.D.,Stout, C.D. (deposition date: 1999-05-19, release date: 2000-03-15, Last modification date: 2023-12-27)

Primary citation

Kresge, N.,Vacquier, V.D.,Stout, C.D.
The high resolution crystal structure of green abalone sperm lysin: implications for species-specific binding of the egg receptor.
J.Mol.Biol., 296:1225-1234, 2000

PubMed Abstract: 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.

PubMed: 10698629
DOI: 10.1006/jmbi.2000.3533

Experimental method

X-RAY DIFFRACTION (1.7 Å)