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http://purl.uniprot.org/citations/37679318http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37679318http://www.w3.org/2000/01/rdf-schema#comment"Carboxysomes are a paradigm of self-assembling proteinaceous organelles found in nature, offering compartmentalisation of enzymes and pathways to enhance carbon fixation. In α-carboxysomes, the disordered linker protein CsoS2 plays an essential role in carboxysome assembly and Rubisco encapsulation. Its mechanism of action, however, is not fully understood. Here we synthetically engineer α-carboxysome shells using minimal shell components and determine cryoEM structures of these to decipher the principle of shell assembly and encapsulation. The structures reveal that the intrinsically disordered CsoS2 C-terminus is well-structured and acts as a universal "molecular thread" stitching through multiple shell protein interfaces. We further uncover in CsoS2 a highly conserved repetitive key interaction motif, [IV]TG, which is critical to the shell assembly and architecture. Our study provides a general mechanism for the CsoS2-governed carboxysome shell assembly and cargo encapsulation and further advances synthetic engineering of carboxysomes for diverse biotechnological applications."xsd:string
http://purl.uniprot.org/citations/37679318http://purl.org/dc/terms/identifier"doi:10.1038/s41467-023-41211-y"xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/author"Jiang Q."xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/author"Shen J."xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/author"Zhang P."xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/author"Zhu Y."xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/author"Liu L.N."xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/author"Huang F."xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/author"Ni T."xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/author"Dou H."xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/author"Dykes G.F."xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/author"Ng P.C."xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/author"Radecke J."xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/name"Nat Commun"xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/pages"5512"xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/title"Intrinsically disordered CsoS2 acts as a general molecular thread for alpha-carboxysome shell assembly."xsd:string
http://purl.uniprot.org/citations/37679318http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/37679318http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/37679318
http://purl.uniprot.org/citations/37679318http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/37679318
http://purl.uniprot.org/uniprot/#_O85041-mappedCitation-37679318http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/37679318
http://purl.uniprot.org/uniprot/#_O85043-mappedCitation-37679318http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/37679318
http://purl.uniprot.org/uniprot/#_P45689-mappedCitation-37679318http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/37679318
http://purl.uniprot.org/uniprot/O85043http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/37679318