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http://purl.uniprot.org/citations/1094461http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1094461http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1094461http://www.w3.org/2000/01/rdf-schema#comment"The three-dimensional structure of the electron transport protein thioredoxin-S2 from E. coli has been determined from a 2.8 A resolution electron density map. The molecule is built up of a central core of three parallel and two antiparallel strands of pleated sheet surrounded by four helices. Thr residues involved in the active center 14-membered disulfide ring of thioredoxin form a protrusion between one of the helices and the middle strand of the pleated sheet. This region of the molecule, comprising two parallel strands joined by the protrusion and a helix, is structurally very similar to corresponding functionally important regions in the nucleotide-binding domains of flavodoxin and the dehydrogenases. The molecule has about 75% of the residues in well-defined secondary structures. The structure indicates that the carboxy-terminal third of the molecule forms an independent folding unit consisting of two strands of antiparallel pleated sheet and a terminal alpha-helix. This agress with the noncovalent reconstitution experiments from thioredoxin peptide fragments. Thioredoxin is an example of a protein with the active center located on a protrusion rather than in a cleft, thus demonstrating the existence of male proteins."xsd:string
http://purl.uniprot.org/citations/1094461http://purl.org/dc/terms/identifier"doi:10.1073/pnas.72.6.2305"xsd:string
http://purl.uniprot.org/citations/1094461http://purl.org/dc/terms/identifier"doi:10.1073/pnas.72.6.2305"xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/author"Eklund H."xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/author"Eklund H."xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/author"Braenden C.-I."xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/author"Braenden C.-I."xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/author"Holmgren A."xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/author"Holmgren A."xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/author"Soederberg B.-O."xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/author"Soederberg B.-O."xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/date"1975"xsd:gYear
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/date"1975"xsd:gYear
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/pages"2305-2309"xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/pages"2305-2309"xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/title"Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8-A resolution."xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/title"Three-dimensional structure of Escherichia coli thioredoxin-S2 to 2.8-A resolution."xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/volume"72"xsd:string
http://purl.uniprot.org/citations/1094461http://purl.uniprot.org/core/volume"72"xsd:string
http://purl.uniprot.org/citations/1094461http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1094461
http://purl.uniprot.org/citations/1094461http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1094461