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The crystal structure of novel chondroitin lyase ODV‐E66, a baculovirus envelope protein
Author(s) -
Kawaguchi Yoshirou,
Sugiura Nobuo,
Kimata Koji,
Kimura Makoto,
Kakuta Yoshimitsu
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.10.021
Subject(s) - lyase , chondroitin , enzyme , biology , biochemistry , chemistry , glycosaminoglycan
Chondroitin lyases have been known as pathogenic bacterial enzymes that degrade chondroitin. Recently, baculovirus envelope protein ODV‐E66 was identified as the first reported viral chondroitin lyase. ODV‐E66 has low sequence identity with bacterial lyases at <12%, and unique characteristics reflecting the life cycle of baculovirus. To understand ODV‐E66's structural basis, the crystal structure was determined and it was found that the structural fold resembled that of polysaccharide lyase 8 proteins and that the catalytic residues were also conserved. This structure enabled discussion of the unique substrate specificity and the stability of ODV‐E66 as well as the host specificity of baculovirus.