Crystal Structure of Chondroitinase B from Flavobacterium heparinumand its Complex with a Disaccharide Product at 1.7 ÅResolution

Authors
Huang, W.
Matte, A.
Li, Y.
Kim, Y.S.
Linhardt, Robert J.
Su, H.
Cygler, M.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
1999
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
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Full Citation
Crystal Structure of Chondroitinase B from Flavobacterium heparinumand its Complex with a Disaccharide Product at 1.7 ÅResolution, W. Huang, A. Matte, Y. Li, Y.S. Kim, R.J. Linhardt, H. Su,M. Cygler, Journal of Molecular Biology, 294, 1257-1269, 1999.
Abstract
Glycosaminoglycans (GAGs) are a family of acidic heteropolysaccharides, including such molecules as chondroitin sulfate, dermatan sulfate, heparin and keratan sulfate. Cleavage of the O-glycosidic bond within GAGs can be accomplished by hydrolases as well as lyases, yielding disaccharide and oligosaccharide products. We have determined the crystal structure of chondroitinase B, a glycosaminoglycan lyase from Flavobacterium heparinum, as well as its complex with a dermatan sulfate disaccharide product, both at 1.7 Å resolution. Chondroitinase B adopts the right-handed parallel β-helix fold, found originally in pectate lyase and subsequently in several polysaccharide lyases and hydrolases. Sequence homology between chondroitinase B and a mannuronate lyase from Pseudomonas sp. suggests this protein also adopts the β-helix fold. Binding of the disaccharide product occurs within a positively charged cleft formed by loops extending from the surface of the β-helix. Amino acid residues responsible for recognition of the disaccharide, as well as potential catalytic residues, have been identified. Two arginine residues, Arg318 and Arg364, are found to interact with the sulfate group attached to O-4 of N-acetylgalactosamine. Cleavage of dermatan sulfate likely occurs at the reducing end of the disaccharide, with Glu333 possibly acting as the general base.
Description
Journal of Molecular Biology, 294, 1257-1269
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
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Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
https://harc.rpi.edu/
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