{"doi":"10.1126/science.1138249","title":"Structural Basis for Substrate Delivery by Acyl Carrier Protein in the Yeast Fatty Acid Synthase","abstract":"<jats:p>\n                    In the multifunctional fungal fatty acid synthase (FAS), the acyl carrier protein (ACP) domain shuttles reaction intermediates covalently attached to its prosthetic phosphopantetheine group between the different enzymatic centers of the reaction cycle. Here, we report the structure of the\n                    <jats:italic>Saccharomyces cerevisiae</jats:italic>\n                    FAS determined at 3.1 angstrom resolution with its ACP stalled at the active site of ketoacyl synthase. The ACP contacts the base of the reaction chamber through conserved, charge-complementary surfaces, which optimally position the ACP toward the catalytic cleft of ketoacyl synthase. The conformation of the prosthetic group suggests a switchblade mechanism for acyl chain delivery to the active site of the enzyme.\n                  </jats:p>","journal":"Science","year":2007,"id":691078,"datarank":0.8027787200214102,"base_score":5.351858133476067,"endowment":5.351858133476067,"self_citation_contribution":0.8027787200214102,"citation_network_contribution":0.0,"self_endowment_contribution":0.8027787200214102,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":210,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":4,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":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":258816,"name":"Simon Jenni","orcid":"0000-0001-5722-5890","position":1,"is_corresponding":false},{"id":1805668,"name":"Christian Frick","orcid":null,"position":2,"is_corresponding":false},{"id":189116,"name":"Nenad Ban","orcid":null,"position":3,"is_corresponding":false},{"id":189115,"name":"Marc Leibundgut","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Structural Basis for Substrate Delivery by Acyl Carrier Protein in the Yeast Fatty Acid Synthase","abstract":"<jats:p>\n                    In the multifunctional fungal fatty acid synthase (FAS), the acyl carrier protein (ACP) domain shuttles reaction intermediates covalently attached to its prosthetic phosphopantetheine group between the different enzymatic centers of the reaction cycle. Here, we report the structure of the\n                    <jats:italic>Saccharomyces cerevisiae</jats:italic>\n                    FAS determined at 3.1 angstrom resolution with its ACP stalled at the active site of ketoacyl synthase. The ACP contacts the base of the reaction chamber through conserved, charge-complementary surfaces, which optimally position the ACP toward the catalytic cleft of ketoacyl synthase. The conformation of the prosthetic group suggests a switchblade mechanism for acyl chain delivery to the active site of the enzyme.\n                  </jats:p>","is_dataset_classified":null,"base_score":5.351858133476067,"endowment":5.351858133476067,"datacite_reuse_total":4,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"17431182","pmcid":null,"openalex_id":"https://openalex.org/W2033443315","authors":[],"funders":[],"total_grants":0,"fwci":8.9363,"citation_percentile":0.98711983,"influential_citations":0,"citation_trend":[{"year":2012,"count":13},{"year":2013,"count":10},{"year":2014,"count":12},{"year":2015,"count":9},{"year":2016,"count":5},{"year":2017,"count":5},{"year":2018,"count":14},{"year":2019,"count":12},{"year":2020,"count":11},{"year":2021,"count":11},{"year":2022,"count":7},{"year":2023,"count":8},{"year":2024,"count":4},{"year":2025,"count":8},{"year":2026,"count":4}],"oa_status":"closed","license":null,"oa_locations":[{"url":"https://www.science.org/doi/pdf/10.1126/science.1138249","host_type":"publisher"},{"url":"https://doi.org/10.1126/science.1138249","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/17431182","host_type":"repository"},{"url":"https://www.dora.lib4ri.ch/psi/islandora/object/psi%3A17873","host_type":"repository"}],"fields_of_study":["Microbial Metabolic Engineering and Bioproduction","Microbial Natural Products and Biosynthesis","Enzyme Catalysis and Immobilization"],"mesh_terms":["Acyl Carrier Protein","Acyltransferases","Amino Acid Sequence","Models, Molecular","Molecular Sequence Data","Protein Binding","Protein Conformation","Protein Structure, Tertiary","Crystallography, X-Ray","Catalytic Domain","Saccharomyces cerevisiae Proteins","Fatty Acid Synthases"],"keywords":["Acyl carrier protein","Fatty acid synthase","ATP synthase","Saccharomyces cerevisiae","Active site","Enzyme","Biochemistry","Chemistry","Yeast","Stereochemistry","Acyl group","Substrate (aquarium)","Fatty acid","Transferase","Biology","Biosynthesis","Organic chemistry"],"sdg_mappings":[],"linked_datasets":[{"doi":"10.6084/m9.figshare.12864899.v1","title":"Additional file 1 of Unstructured regions of large enzymatic complexes control the availability of metabolites with signaling functions","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.12864899","title":"Additional file 1 of Unstructured regions of large enzymatic complexes control the availability of metabolites with signaling functions","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.20113945.v1","title":"Additional file 1 of Solution structure of the type I polyketide synthase Pks13 from Mycobacterium tuberculosis","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.20113945","title":"Additional file 1 of Solution structure of the type I polyketide synthase Pks13 from Mycobacterium tuberculosis","publisher":"figshare","resource_type":"JournalArticle"}],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-27T18:51:25.890230Z","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":[]}