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.
| Original language | English |
|---|---|
| Pages (from-to) | 3943-3948 |
| Number of pages | 6 |
| Journal | FEBS Letters |
| Volume | 587 |
| Issue number | 24 |
| DOIs | |
| Publication status | Published - Dec 11 2013 |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Biophysics
- Cell Biology
- Genetics
- Molecular Biology
- Structural Biology
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Cite this
Kawaguchi, Y., Sugiura, N., Kimata, K., Kimura, M., & Kakuta, Y. (2013). The crystal structure of novel chondroitin lyase ODV-E66, a baculovirus envelope protein. FEBS Letters, 587(24), 3943-3948. https://doi.org/10.1016/j.febslet.2013.10.021