The high resolution crystal structure of green abalone sperm lysin: implications for species-specific binding of the egg receptor 1 1Edited by R. Huber

摘要: Abstract Abalone sperm lysin is a 16 kDa acrosomal protein used by to create hole in the egg vitelline envelope. Lysins from seven California abalone exhibit species-specificity binding their receptor, and range sequence identity 63 % 90 %. The crystal structure of dimer Haliotis fulgens (green abalone) has been determined 1.71 A multiple isomorphous replacement. Comparisons with rufescens (red reveal similar overall fold conservation features contributing lysin’s amphipathic character. two structures do, however, differences surface residues electrostatics. large clustering non-conserved around waist clefts dimer, charged these regions, indicate areas molecule which may be involved species-specific recognition.