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

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

Research output: Contribution to journalArticle

12 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 languageEnglish
Pages (from-to)3943-3948
Number of pages6
JournalFEBS Letters
Volume587
Issue number24
DOIs
Publication statusPublished - Dec 11 2013

Fingerprint

Chondroitin Lyases
Baculoviridae
Polysaccharide-Lyases
Crystal structure
Chondroitin
Lyases
Life cycle
Proteins
Host Specificity
Substrate Specificity
Life Cycle Stages
Substrates
Enzymes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

Cite this

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 journalArticle

Kawaguchi, Yoshirou ; Sugiura, Nobuo ; Kimata, Koji ; Kimura, Makoto ; Kakuta, Yoshimitsu. / The crystal structure of novel chondroitin lyase ODV-E66, a baculovirus envelope protein. In: FEBS Letters. 2013 ; Vol. 587, No. 24. pp. 3943-3948.
@article{6deb5043959540f590d2b9481c3ad1f8,
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.",
author = "Yoshirou Kawaguchi and Nobuo Sugiura and Koji Kimata and Makoto Kimura and Yoshimitsu Kakuta",
year = "2013",
month = "12",
day = "11",
doi = "10.1016/j.febslet.2013.10.021",
language = "English",
volume = "587",
pages = "3943--3948",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "24",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=84888639854&partnerID=8YFLogxK

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 -