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

FEBS Lett. 2013 Oct 25:S0014-5793(13)00778-3. doi: 10.1016/j.febslet.2013.10.021. Online ahead of print.

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.

Keywords: Autographa californica; Chondroitin sulfate; Interdomain movement; ODV-E66; PL8; Polysaccharide lyase; occlusion derived virus envelope protein 66; polysaccharide lyase 8; β-Elimination.