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Crystallization and X-ray diffraction analysis of chondroitin lyase from baculovirus: envelope protein ODV-E66.

ABSTRACT: Baculovirus envelope protein ODV-E66 (67-704), in which the N-terminal 66 amino acids are truncated, is a chondroitin lyase. It digests chondroitin and chondroitin 6-sulfate efficiently, but does not digest chondroitin 4-sulfate. This unique characteristic is useful for the preparation of specific chondroitin oligosaccharides and for investigation of the mechanism of baculovirus infection. ODV-E66 (67-704) was crystallized; the crystal diffracted to 1.8 Å resolution and belonged to space group P6(2) or P6(4), with unit-cell parameters a = b = 113.5, c = 101.5 Å. One molecule is assumed to be present per asymmetric unit, which gives a Matthews coefficient of 2.54 Å(3) Da(-1).

SUBMITTER: Kawaguchi Y

PROVIDER: S-EPMC3274400 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature

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Crystallization and X-ray diffraction analysis of chondroitin lyase from baculovirus: envelope protein ODV-E66.

Kawaguchi Yoshirou Y Sugiura Nobuo N Onishi Momo M Kimata Koji K Kimura Makoto M Kakuta Yoshimitu Y

Acta crystallographica. Section F, Structural biology and crystallization communications 20120126 Pt 2

Baculovirus envelope protein ODV-E66 (67-704), in which the N-terminal 66 amino acids are truncated, is a chondroitin lyase. It digests chondroitin and chondroitin 6-sulfate efficiently, but does not digest chondroitin 4-sulfate. This unique characteristic is useful for the preparation of specific chondroitin oligosaccharides and for investigation of the mechanism of baculovirus infection. ODV-E66 (67-704) was crystallized; the crystal diffracted to 1.8 Å resolution and belonged to space group P ...[more]

PMID: 22297996

Similar Datasets

Baculovirus envelope protein ODV-E66 is a novel chondroitinase with distinct substrate specificity.

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