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Updated: May 3, 2026

Microcrystallography of Protein Crystals and In Cellulo Diffraction
Published on: July 21, 2017
The crystal structure of novel chondroitin lyase ODV-E66, a baculovirus envelope protein
Yoshirou Kawaguchi1, Nobuo Sugiura2, Koji Kimata3
1Laboratory of Structural Biology, Graduate School of System Life Sciences, Kyushu University, 6-10-1 Hakozaki, Fukuoka 812-8581, Japan.
Abstract:
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.
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