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http://purl.uniprot.org/citations/23071318http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23071318http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23071318http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/23071318http://www.w3.org/2000/01/rdf-schema#comment"Acetylation of lysine residues is an important posttranslational modification found in all domains of life. α-Tubulin is specifically acetylated on lysine 40, a modification that serves to stabilize microtubules of axons and cilia. Whereas histone acetyltransferases have been extensively studied, there is no structural and mechanistic information available on α-tubulin acetyltransferases. Here, we present the structure of the human α-tubulin acetyltransferase catalytic domain bound to its cosubstrate acetyl-CoA at 1.05 Å resolution. Compared with other lysine acetyltransferases of known structure, α-tubulin acetyltransferase displays a relatively well-conserved cosubstrate binding pocket but is unique in its active site and putative α-tubulin binding site. Using acetylation assays with structure-guided mutants, we map residues important for acetyl-CoA binding, substrate binding, and catalysis. This analysis reveals a basic patch implicated in substrate binding and a conserved glutamine residue required for catalysis, demonstrating that the family of α-tubulin acetyltransferases uses a reaction mechanism different from other lysine acetyltransferases characterized to date."xsd:string
http://purl.uniprot.org/citations/23071318http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1209343109"xsd:string
http://purl.uniprot.org/citations/23071318http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1209343109"xsd:string
http://purl.uniprot.org/citations/23071318http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1209343109"xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/author"Lorentzen E."xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/author"Lorentzen E."xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/author"Vetter M."xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/author"Vetter M."xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/author"Taschner M."xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/author"Taschner M."xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/pages"19649-19654"xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/pages"19649-19654"xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/title"Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA."xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/title"Atomic resolution structure of human alpha-tubulin acetyltransferase bound to acetyl-CoA."xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/volume"109"xsd:string
http://purl.uniprot.org/citations/23071318http://purl.uniprot.org/core/volume"109"xsd:string
http://purl.uniprot.org/citations/23071318http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23071318
http://purl.uniprot.org/citations/23071318http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23071318