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

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

All Science Journal Classification (ASJC) codes

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

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