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 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Biophysics
- Cell Biology
- Genetics
- Molecular Biology
- Structural Biology
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The crystal structure of novel chondroitin lyase ODV-E66, a baculovirus envelope protein. / Kawaguchi, Yoshirou; Sugiura, Nobuo; Kimata, Koji; Kimura, Makoto; Kakuta, Yoshimitsu.
In: FEBS Letters, Vol. 587, No. 24, 11.12.2013, p. 3943-3948.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The crystal structure of novel chondroitin lyase ODV-E66, a baculovirus envelope protein
AU - Kawaguchi, Yoshirou
AU - Sugiura, Nobuo
AU - Kimata, Koji
AU - Kimura, Makoto
AU - Kakuta, Yoshimitsu
PY - 2013/12/11
Y1 - 2013/12/11
N2 - 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.
AB - 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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UR - http://www.scopus.com/inward/citedby.url?scp=84888639854&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2013.10.021
DO - 10.1016/j.febslet.2013.10.021
M3 - Article
AN - SCOPUS:84888639854
VL - 587
SP - 3943
EP - 3948
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 24
ER -