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http://purl.uniprot.org/citations/37468522http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37468522http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/37468522http://www.w3.org/2000/01/rdf-schema#comment"G-proteins function as molecular switches to power cofactor translocation and confer fidelity in metal trafficking. The G-protein, MMAA, together with MMAB, an adenosyltransferase, orchestrate cofactor delivery and repair of B12-dependent human methylmalonyl-CoA mutase (MMUT). The mechanism by which the complex assembles and moves a >1300 Da cargo, or fails in disease, are poorly understood. Herein, we report the crystal structure of the human MMUT-MMAA nano-assembly, which reveals a dramatic 180° rotation of the B12 domain, exposing it to solvent. The complex, stabilized by MMAA wedging between two MMUT domains, leads to ordering of the switch I and III loops, revealing the molecular basis of mutase-dependent GTPase activation. The structure explains the biochemical penalties incurred by methylmalonic aciduria-causing mutations that reside at the MMAA-MMUT interfaces we identify here."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.org/dc/terms/identifier"doi:10.1038/s41467-023-40077-4"xsd:string
http://purl.uniprot.org/citations/37468522http://purl.org/dc/terms/identifier"doi:10.1038/s41467-023-40077-4"xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/author"Banerjee R."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/author"Banerjee R."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/author"Gouda H."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/author"Gouda H."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/author"Ruetz M."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/author"Ruetz M."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/author"Mascarenhas R."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/author"Mascarenhas R."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/author"Heitman N."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/author"Heitman N."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/author"Yaw M."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/author"Yaw M."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/date"2023"xsd:gYear
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/name"Nat. Commun."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/name"Nat Commun"xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/pages"4332"xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/pages"4332"xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/title"Architecture of the human G-protein-methylmalonyl-CoA mutase nanoassembly for B12 delivery and repair."xsd:string
http://purl.uniprot.org/citations/37468522http://purl.uniprot.org/core/title"Architecture of the human G-protein-methylmalonyl-CoA mutase nanoassembly for B12 delivery and repair."xsd:string