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http://purl.uniprot.org/citations/7937966http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7937966http://www.w3.org/2000/01/rdf-schema#comment"A jellyroll beta-sandwich protein, the Bacillus beta-glucanase H(A16-M), is used to probe the role of N-terminal peptide regions in protein folding in vivo. A gene encoding H(A16-M) is rearranged to place residues 1-58 of the protein behind a signal peptide and residues 59-214. The rearranged gene is expressed in Escherichia coli. The resultant circularly permuted protein, cpA16M-59, is secreted into the periplasm, correctly processed, and folded into a stable and active enzyme. Crystal structure analysis at 2.0-A resolution, R = 15.3%, shows cpA16M-59 to have a three-dimensional structure nearly identical with that of the parent beta-glucanase. An analogous experiment based on the wild-type Bacillus macerans beta-glucanase, giving rise to the circularly permuted variant cpMAC-57, yields the same results. Folding of these proteins, therefore, is not a vectorial process depending on the conformation adopted by their native N-terminal oligopeptides after ribosomal synthesis and translocation through the cytoplasmic membrane."xsd:string
http://purl.uniprot.org/citations/7937966http://purl.org/dc/terms/identifier"doi:10.1073/pnas.91.22.10417"xsd:string
http://purl.uniprot.org/citations/7937966http://purl.uniprot.org/core/author"Borriss R."xsd:string
http://purl.uniprot.org/citations/7937966http://purl.uniprot.org/core/author"Piotukh K."xsd:string
http://purl.uniprot.org/citations/7937966http://purl.uniprot.org/core/author"Hahn M."xsd:string
http://purl.uniprot.org/citations/7937966http://purl.uniprot.org/core/author"Heinemann U."xsd:string
http://purl.uniprot.org/citations/7937966http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/7937966http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/7937966http://purl.uniprot.org/core/pages"10417-10421"xsd:string
http://purl.uniprot.org/citations/7937966http://purl.uniprot.org/core/title"Native-like in vivo folding of a circularly permuted jellyroll protein shown by crystal structure analysis."xsd:string
http://purl.uniprot.org/citations/7937966http://purl.uniprot.org/core/volume"91"xsd:string
http://purl.uniprot.org/citations/7937966http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7937966
http://purl.uniprot.org/citations/7937966http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7937966
http://purl.uniprot.org/uniprot/#_P23904-mappedCitation-7937966http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/7937966
http://purl.uniprot.org/uniprot/P23904http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/7937966