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http://purl.uniprot.org/citations/30785395http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30785395http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30785395http://www.w3.org/2000/01/rdf-schema#comment"SETD3 is a member of the SET (Su(var)3-9, Enhancer of zeste, and Trithorax) domain protein superfamily and plays important roles in hypoxic pulmonary hypertension, muscle differentiation, and carcinogenesis. Previously, we identified SETD3 as the actin-specific methyltransferase that methylates the N3 of His73 on β-actin (Kwiatkowski et al., 2018). Here, we present two structures of S-adenosyl-L-homocysteine-bound SETD3 in complex with either an unmodified β-actin peptide or its His-methylated variant. Structural analyses, supported by biochemical experiments and enzyme activity assays, indicate that the recognition and methylation of β-actin by SETD3 are highly sequence specific, and that both SETD3 and β-actin adopt pronounced conformational changes upon binding to each other. In conclusion, this study is the first to show a catalytic mechanism of SETD3-mediated histidine methylation on β-actin, which not only throws light on the protein histidine methylation phenomenon but also facilitates the design of small molecule inhibitors of SETD3."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.org/dc/terms/identifier"doi:10.7554/elife.43676"xsd:string
http://purl.uniprot.org/citations/30785395http://purl.org/dc/terms/identifier"doi:10.7554/elife.43676"xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Wu G."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Wu G."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Xu C."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Xu C."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Yu H."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Yu H."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Tu X."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Tu X."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Min J."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Min J."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Liao S."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Liao S."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Guo Q."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Guo Q."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Drozak J."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Drozak J."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Kwiatkowski S."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Kwiatkowski S."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Tomaka W."xsd:string
http://purl.uniprot.org/citations/30785395http://purl.uniprot.org/core/author"Tomaka W."xsd:string