{"doi":"10.1073/pnas.1209343109","title":"Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA","abstract":"<jats:p>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.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":2012,"id":14619,"datarank":2.429253866160264,"base_score":3.8066624897703196,"endowment":3.8066624897703196,"self_citation_contribution":0.5709993734655481,"citation_network_contribution":1.858254492694716,"self_endowment_contribution":0.5709993734655481,"citer_contribution":1.858254492694716,"corpus_percentile":null,"corpus_rank":null,"citation_count":44,"citer_count":43,"citers_with_citation_signal":41,"citers_with_endowment":41,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":114686,"name":"Melanie Vetter","orcid":null,"position":1,"is_corresponding":false},{"id":114687,"name":"Esben Lorentzen","orcid":null,"position":2,"is_corresponding":false},{"id":114685,"name":"Michael Taschner","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":3.8066624897703196,"endowment":3.8066624897703196,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"23071318","pmcid":"PMC3511736","openalex_id":"https://openalex.org/W2016961165","authors":[],"funders":[{"funder_name":"European Research Council","grant_id":"310343","title":"Structural Studies and Regulation of Intraflagellar Transport Complexes"},{"funder_name":"Austrian Science Fund (FWF)","grant_id":"J 3148","title":"Structural analysis of Intraflagellar 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and proteasome pathways","Peptidase Inhibition and Analysis","Histone Deacetylase Inhibitors Research","Biology","Medicine","Chemistry","0301 basic medicine","03 medical and health sciences","Acetyl Coenzyme A","Acetyltransferases","Biocatalysis","Crystallography, X-Ray","Humans","Models, Molecular","Protein Binding","Protein Conformation"],"mesh_terms":["Acetyl Coenzyme A","Acetyltransferases","Humans","Models, Molecular","Protein Binding","Protein Conformation","Crystallography, X-Ray","Biocatalysis"],"keywords":["Acetyltransferases","Acetyltransferase","Acetylation","Histone Acetyltransferases","Biochemistry","Lysine","PCAF","Tubulin","P300-CBP Transcription Factors","Chemistry","Histone acetyltransferase","Active site","Transferase","Cofactor","Biology","Enzyme","Microtubule","Amino acid","Cell biology","Models, Molecular","Acetyl Coenzyme A","Protein Conformation","Biocatalysis","Humans","Crystallography, X-Ray","Protein Binding"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-06-01T13:04:09.982173Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}