DESCRIBE <http://purl.uniprot.org/citations/7490746>

Subject	Predicate	Object
http://purl.uniprot.org/citations/7490746	http://www.w3.org/1999/02/22-rdf-syntax-ns#type	http://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7490746	http://www.w3.org/1999/02/22-rdf-syntax-ns#type	http://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7490746	http://www.w3.org/2000/01/rdf-schema#comment	"Seeds of Canavalia ensiformis (jack bean) contain besides large amounts of canavalin and concanavalin A, a protein with a molecular mass of 33,800 which has been named concanavalin B. Although concanavalin B shares about 40% sequence identity with plant chitinases belonging to glycosyl hydrolase family 18, no chitinase activity could be detected for this protein. To resolve this incongruity concanavalin B was crystallised and its three-dimensional structure determined at 1.65 A (1 A = 0.1 nm) resolution. The structure consists of a single domain with a (beta/alpha)8 topology. A 30 amino acid residue long loop occurs between the second beta-strand of the barrel and the second alpha-helix. This extended loop is unusual for the (beta/alpha)8 topology, but appears in a similar conformation in the structures of the seed protein narbonin and several chitinases as well. Two non-proline cis-peptide bonds are present in the structure of concanavalin B: Ser34-Phe, and Trp265-Asn. This structural feature is rarely observed in proteins, but could also be identified in the three-dimensional structures of family 18 chitinases and narbonin in coincident positions. In the chitinases the aromatic residues of the non-proline cis-peptides have been proposed to have a function in the binding of the substrate. The region in concanavalin B, where in chitinases the active site is located, shows two significant differences. First, the catalytic glutamic acid is a glutamine in concanavalin B. Second, although part of the substrate binding cleft of the chitinases is present in concanavalin B, it is much shorter. From this we conclude that concanavalin B and family 18 chitinases are closely related, but that concanavalin B has lost its enzymatic function. It still may act as a carbohydrate binding protein, however."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.org/dc/terms/identifier	"doi:10.1006/jmbi.1995.0614"xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.org/dc/terms/identifier	"doi:10.1006/jmbi.1995.0614"xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/author	"Jansonius J.N."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/author	"Jansonius J.N."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/author	"Hennig M."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/author	"Hennig M."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/author	"Dijkstra B.W."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/author	"Dijkstra B.W."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/author	"van Scheltinga A.C.T."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/author	"van Scheltinga A.C.T."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/author	"Schlesier B."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/author	"Schlesier B."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/date	"1995"xsd:gYear
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/date	"1995"xsd:gYear
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/name	"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/name	"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/pages	"237-246"xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/pages	"237-246"xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/title	"Crystal structure of concanavalin B at 1.65-A resolution. An 'inactivated' chitinase from seeds of Canavalia ensiformis."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/title	"Crystal structure of concanavalin B at 1.65-A resolution. An 'inactivated' chitinase from seeds of Canavalia ensiformis."xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/volume	"254"xsd:string
http://purl.uniprot.org/citations/7490746	http://purl.uniprot.org/core/volume	"254"xsd:string