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http://purl.uniprot.org/citations/32123388http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32123388http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32123388http://www.w3.org/2000/01/rdf-schema#comment"Carboxysomes are bacterial microcompartments that function as the centerpiece of the bacterial CO2-concentrating mechanism by facilitating high CO2 concentrations near the carboxylase Rubisco. The carboxysome self-assembles from thousands of individual proteins into icosahedral-like particles with a dense enzyme cargo encapsulated within a proteinaceous shell. In the case of the α-carboxysome, there is little molecular insight into protein-protein interactions that drive the assembly process. Here, studies on the α-carboxysome from Halothiobacillus neapolitanus demonstrate that Rubisco interacts with the N terminus of CsoS2, a multivalent, intrinsically disordered protein. X-ray structural analysis of the CsoS2 interaction motif bound to Rubisco reveals a series of conserved electrostatic interactions that are only made with properly assembled hexadecameric Rubisco. Although biophysical measurements indicate that this single interaction is weak, its implicit multivalency induces high-affinity binding through avidity. Taken together, our results indicate that CsoS2 acts as an interaction hub to condense Rubisco and enable efficient α-carboxysome formation."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.org/dc/terms/identifier"doi:10.1038/s41594-020-0387-7"xsd:string
http://purl.uniprot.org/citations/32123388http://purl.org/dc/terms/identifier"doi:10.1038/s41594-020-0387-7"xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/author"Oltrogge L.M."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/author"Oltrogge L.M."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/author"Savage D.F."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/author"Savage D.F."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/author"Chaijarasphong T."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/author"Chaijarasphong T."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/author"Chen A.W."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/author"Chen A.W."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/author"Bolin E.R."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/author"Bolin E.R."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/author"Marqusee S."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/author"Marqusee S."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/pages"281-287"xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/pages"281-287"xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/title"Multivalent interactions between CsoS2 and Rubisco mediate alpha-carboxysome formation."xsd:string
http://purl.uniprot.org/citations/32123388http://purl.uniprot.org/core/title"Multivalent interactions between CsoS2 and Rubisco mediate alpha-carboxysome formation."xsd:string