The crystal structure of novel chondroitin lyase ODV-E66, a baculovirus envelope protein

Yoshirou Kawaguchi; Nobuo Sugiura; Koji Kimata; Makoto Kimura; Yoshimitsu Kakuta

doi:10.1016/j.febslet.2013.10.021

The crystal structure of novel chondroitin lyase ODV-E66, a baculovirus envelope protein

Yoshirou Kawaguchi, Nobuo Sugiura, Koji Kimata, Makoto Kimura, Yoshimitsu Kakuta

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

13 Citations (Scopus)

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	https://doi.org/10.1016/j.febslet.2013.10.021
Publication status	Published - Dec 11 2013

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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title = "The crystal structure of novel chondroitin lyase ODV-E66, a baculovirus envelope protein",

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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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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The crystal structure of novel chondroitin lyase ODV-E66, a baculovirus envelope protein

Abstract

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