The crystal structure of novel chondroitin lyase ODV-E66, a baculovirus envelope protein.
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.
Yoshirou
Y
Kawaguchi
Nobuo
N
Sugiura
Koji
K
Kimata
Makoto
M
Kimura
Yoshimitsu
Y
Kakuta
D000595:Amino Acid Sequence; D016367:Baculoviridae / Q000201:enzymology* / Q000235:genetics; D002808:Chondroitin Lyases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018360:Crystallography, X-Ray; D004252:DNA Mutational Analysis; D004795:Enzyme Stability; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017386:Sequence Homology, Amino Acid; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D014759:Viral Envelope Proteins; D002808:Chondroitin Lyases