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http://purl.uniprot.org/citations/22831795http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22831795http://www.w3.org/2000/01/rdf-schema#comment"The substrate-binding mode of a 26-kDa GH19 chitinase from rye, Secale cereale, seeds (RSC-c) was investigated by crystallography, site-directed mutagenesis and NMR spectroscopy. The crystal structure of RSC-c in a complex with an N-acetylglucosamine tetramer, (GlcNAc)(4) , was successfully solved, and revealed the binding mode of the tetramer to be an aglycon-binding site, subsites +1, +2, +3, and +4. These are the first crystallographic data showing the oligosaccharide-binding mode of a family GH19 chitinase. From HPLC analysis of the enzymatic reaction products, mutation of Trp72 to alanine was found to affect the product distribution obtained from the substrate, p-nitrophenyl penta-N-acetyl-β-chitopentaoside. Mutational experiments confirmed the crystallographic finding that the Trp72 side chain interacts with the +4 moiety of the bound substrate. To further confirm the crystallographic data, binding experiments were also conducted in solution using NMR spectroscopy. Several signals in the (1) H-(15) N HSQC spectrum of the stable isotope-labeled RSC-c were affected upon addition of (GlcNAc)(4) . Signal assignments revealed that most signals responsive to the addition of (GlcNAc)(4) are derived from amino acids located at the surface of the aglycon-binding site. The binding mode deduced from NMR binding experiments in solution was consistent with that from the crystal structure."xsd:string
http://purl.uniprot.org/citations/22831795http://purl.org/dc/terms/identifier"doi:10.1111/j.1742-4658.2012.08723.x"xsd:string
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/author"Fukuda T."xsd:string
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/author"Kondo K."xsd:string
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/author"Okazaki Y."xsd:string
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/author"Inanaga H."xsd:string
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/author"Numata T."xsd:string
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/author"Osawa T."xsd:string
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/author"Fukamizo T."xsd:string
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/author"Ohnuma T."xsd:string
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/author"Shinya S."xsd:string
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/name"FEBS J"xsd:string
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/pages"3639-3651"xsd:string
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/title"Crystal structure and chitin oligosaccharide-binding mode of a 'loopful' family GH19 chitinase from rye, Secale cereale, seeds."xsd:string
http://purl.uniprot.org/citations/22831795http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/22831795http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22831795
http://purl.uniprot.org/citations/22831795http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22831795
http://purl.uniprot.org/uniprot/#_Q9FRV0-mappedCitation-22831795http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22831795
http://purl.uniprot.org/uniprot/Q9FRV0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22831795