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

    Author
    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
    Date Issued
    1999
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/;
    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.
    Metadata
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    URI
    https://doi.org/10.1006/jmbi.1999.3292; https://hdl.handle.net/20.500.13015/5874
    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; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
    Department
    The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; https://harc.rpi.edu/;
    Access
    https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1006/jmbi.1999.3292;
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