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dc.contributor.authorHuang, W.
dc.contributor.authorMatte, A.
dc.contributor.authorLi, Y.
dc.contributor.authorKim, Y.S.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorSu, H.
dc.contributor.authorCygler, M.
dc.date1999
dc.date.accessioned2022-06-27T16:21:11Z
dc.date.available2022-06-27T16:21:11Z
dc.date.issued1999
dc.identifier.citationCrystal 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.
dc.identifier.urihttps://doi.org/10.1006/jmbi.1999.3292
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5874
dc.descriptionJournal of Molecular Biology, 294, 1257-1269
dc.descriptionNote : 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.
dc.description.abstractGlycosaminoglycans (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.
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1006/jmbi.1999.3292
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleCrystal Structure of Chondroitinase B from Flavobacterium heparinumand its Complex with a Disaccharide Product at 1.7 ÅResolution
dc.typeArticle
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dcterms.isVersionOfhttps://doi.org/10.1006/jmbi.1999.3292
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dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)


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