Literature DB >> 24446551

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

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

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.
© 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Year:  2013        PMID: 24446551

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  7 in total

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5.  Substrate specificity of Chondroitinase ABC I based on analyses of biochemical reactions and crystal structures in complex with disaccharides.

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Journal:  Glycobiology       Date:  2021-12-18       Impact factor: 4.313

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Journal:  Sci Rep       Date:  2018-06-12       Impact factor: 4.379

  7 in total

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