Open AccessThe tertiary structure of an i‐type lysozyme isolated from the common orient clam ( Meretrix lusoria )
Author(s) -
Kuwano Yuko,
Yoneda Kazunari,
Kawaguchi Yuya,
Araki Tomohiro
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113028170
Subject(s) - lysozyme , trimer , protein tertiary structure , residue (chemistry) , chemistry , enzyme , dimer , amino acid , aspartic acid , biochemistry , amino acid residue , stereochemistry , peptide sequence , biology , organic chemistry , gene
To evaluate the structure–function relationships of invertebrate lysozymes, a new invertebrate‐type (i‐type) lysozyme was isolated from the common orient clam ( Meretrix lusoria ) and the tertiary structure of this enzyme was determined. Comparison of the tertiary structure of this enzyme with those of chicken and Venerupi philippinarum lysozymes revealed that the location of the side chain of the second catalytic residue, an aspartic acid, and the N ‐acetylglucosamine trimer bound at subsites A – C were different. Furthermore, the amino acid electrostatically interacting with Asp30 in V. philippinarum lysozyme, Lys108, was substituted by Gly in M. lusoria lysozyme and no other possible amino acid that could contribute to this interaction was found in M. lusoria lysozyme. It therefore seems that the substitutions of the amino acids at the interface of the V. philippinarum lysozyme dimer are likely to change the oligomeric state of the M. lusoria lysozyme.