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http://purl.uniprot.org/citations/14638692http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14638692http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14638692http://www.w3.org/2000/01/rdf-schema#comment"The subunits of the dihydrolipoyl acetyltransferase (E2) component of mammalian pyruvate dehydrogenase complex can form a 60-mer via association of the C-terminal I domain of E2 at the vertices of a dodecahedron. Exterior to this inner core structure, E2 has a pyruvate dehydrogenase component (E1)-binding domain followed by two lipoyl domains, all connected by mobile linker regions. The assembled core structure of mammalian pyruvate dehydrogenase complex also includes the dihydrolipoyl dehydrogenase (E3)-binding protein (E3BP) that binds the I domain of E2 by its C-terminal I' domain. E3BP similarly has linker regions connecting an E3-binding domain and a lipoyl domain. The composition of E2.E3BP was thought to be 60 E2 plus approximately 12 E3BP. We have prepared homogenous human components. E2 and E2.E3BP have s(20,w) values of 36 S and 31.8 S, respectively. Equilibrium sedimentation and small angle x-ray scattering studies indicate that E2.E3BP has lower total mass than E2, and small angle x-ray scattering showed that E3 binds to E2.E3BP outside the central dodecahedron. In the presence of saturating levels of E1, E2 bound approximately 60 E1 and maximally sedimented 64.4 +/-1.5 S faster than E2, whereas E1-saturated E2.E3BP maximally sedimented 49.5 +/-1.4 S faster than E2.E3BP. Based on the impact on sedimentation rates by bound E1, we estimate fewer E1 (approximately 12) were bound by E2.E3BP than by E2. The findings of a smaller E2.E3BP mass and a lower capacity to bind E1 support the smaller E3BP substituting for E2 subunits rather than adding to the 60-mer. We describe a substitution model in which 12 I' domains of E3BP replace 12 I domains of E2 by forming 6 dimer edges that are symmetrically located in the dodecahedron structure. Twelve E3 dimers were bound per E248.E3BP12 mass, which is consistent with this model."xsd:string
http://purl.uniprot.org/citations/14638692http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m308172200"xsd:string
http://purl.uniprot.org/citations/14638692http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m308172200"xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/author"Fujisawa T."xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/author"Fujisawa T."xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/author"Aso Y."xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/author"Aso Y."xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/author"Hiromasa Y."xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/author"Hiromasa Y."xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/author"Roche T.E."xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/author"Roche T.E."xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/pages"6921-6933"xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/pages"6921-6933"xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/title"Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components."xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/title"Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components."xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/14638692http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/14638692http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14638692
http://purl.uniprot.org/citations/14638692http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/14638692
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