{"doi":"10.1110/ps.051415905","title":"Crystal structure of yeast YHR049W/FSH1, a member of the serine hydrolase family","abstract":"<jats:title>Abstract</jats:title><jats:p>Yhr049w/FSH1 was recently identified in a combined computational and experimental proteomics analysis for the detection of active serine hydrolases in yeast. This analysis suggested that FSH1 might be a serine‐type hydrolase belonging to the broad functional αβ‐hydrolase superfamily. In order to get insight into the molecular function of this gene, it was targeted in our yeast structural genomics project. The crystal structure of the protein confirms that it contains a Ser/His/Asp catalytic triad that is part of a minimal α/β‐hydrolase fold. The architecture of the putative active site and analogies with other protein structures suggest that FSH1 may be an esterase. This finding was further strengthened by the unexpected presence of a compound covalently bound to the catalytic serine in the active site. Apparently, the enzyme was trapped with a reactive compound during the purification process.</jats:p>","journal":"Protein Science","year":2005,"id":652639,"datarank":0.4636563680037475,"base_score":3.091042453358316,"endowment":3.091042453358316,"self_citation_contribution":0.4636563680037475,"citation_network_contribution":0.0,"self_endowment_contribution":0.4636563680037475,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":21,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"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":110954,"name":"Nicolas Leulliot","orcid":null,"position":1,"is_corresponding":false},{"id":1702559,"name":"Marc Graille","orcid":null,"position":2,"is_corresponding":false},{"id":1702560,"name":"Nadège Hervouet","orcid":null,"position":3,"is_corresponding":false},{"id":1702561,"name":"Frank Coste","orcid":null,"position":4,"is_corresponding":false},{"id":1702562,"name":"Hélène Bénédetti","orcid":null,"position":5,"is_corresponding":false},{"id":1702563,"name":"Charles Zelwer","orcid":null,"position":6,"is_corresponding":false},{"id":1702564,"name":"Joel Janin","orcid":null,"position":7,"is_corresponding":false},{"id":1702565,"name":"Herman Van Tilbeurgh","orcid":null,"position":8,"is_corresponding":false},{"id":1702557,"name":"Sophie Quevillon‐Cheruel","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Crystal structure of yeast YHR049W/FSH1, a member of the serine hydrolase family","abstract":"<jats:title>Abstract</jats:title><jats:p>Yhr049w/FSH1 was recently identified in a combined computational and experimental proteomics analysis for the detection of active serine hydrolases in yeast. This analysis suggested that FSH1 might be a serine‐type hydrolase belonging to the broad functional αβ‐hydrolase superfamily. In order to get insight into the molecular function of this gene, it was targeted in our yeast structural genomics project. The crystal structure of the protein confirms that it contains a Ser/His/Asp catalytic triad that is part of a minimal α/β‐hydrolase fold. The architecture of the putative active site and analogies with other protein structures suggest that FSH1 may be an esterase. This finding was further strengthened by the unexpected presence of a compound covalently bound to the catalytic serine in the active site. Apparently, the enzyme was trapped with a reactive compound during the purification process.</jats:p>","is_dataset_classified":null,"base_score":3.091042453358316,"endowment":3.091042453358316,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"15802654","pmcid":"PMC2253265","openalex_id":"https://openalex.org/W2027387267","authors":[],"funders":[],"total_grants":0,"fwci":0.5519,"citation_percentile":0.62842054,"influential_citations":0,"citation_trend":[{"year":2012,"count":1},{"year":2013,"count":1},{"year":2015,"count":1},{"year":2017,"count":2},{"year":2019,"count":4},{"year":2020,"count":3},{"year":2021,"count":2},{"year":2023,"count":1},{"year":2024,"count":1}],"oa_status":"bronze","license":"http://onlinelibrary.wiley.com/termsAndConditions#vor","oa_locations":[{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1110/ps.051415905","host_type":"journal"},{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1110/ps.051415905","host_type":"publisher"},{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1110%2Fps.051415905","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.051415905","host_type":"publisher"},{"url":"https://doi.org/10.1110/ps.051415905","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/15802654","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/2253265","host_type":"repository"}],"fields_of_study":["Enzyme Structure and Function","Enzyme Production and Characterization","Amino Acid Enzymes and Metabolism"],"mesh_terms":["Amino Acid Sequence","Cloning, Molecular","Fungal Proteins","Hydrolases","Models, Molecular","Molecular Sequence Data","Saccharomyces cerevisiae","Sequence Homology, Amino Acid","Crystallography, X-Ray"],"keywords":["Serine hydrolase","Hydrolase","Serine","Catalytic triad","Structural genomics","Active site","Yeast","Esterase","Biochemistry","Biology","Enzyme","Chemistry","Protein structure"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Clean water and sanitation"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-10T16:20:41.349142Z","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":[]}