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http://purl.uniprot.org/citations/18596200http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18596200http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18596200http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/18596200http://www.w3.org/2000/01/rdf-schema#comment"The three ribosomal proteins L7, S5, and S18 are included in the rare subset of prokaryotic proteins that are known to be N(alpha)-acetylated. The GCN5-related N-acetyltransferase (GNAT) protein RimI, responsible for the N(alpha)-acetylation of the ribosomal protein S18, was cloned from Salmonella typhimurium LT2 (RimI(ST)), overexpressed, and purified to homogeneity. Steady-state kinetic parameters for RimI(ST) were determined for AcCoA and a peptide substrate consisting of the first six amino acids of the target protein S18. The crystal structure of RimI(ST) was determined in complex with CoA, AcCoA, and a CoA-S-acetyl-ARYFRR bisubstrate inhibitor. The structures are consistent with a direct nucleophilic addition-elimination mechanism with Glu103 and Tyr115 acting as the catalytic base and acid, respectively. The RimI(ST)-bisubstrate complex suggests that several residues change conformation upon interacting with the N terminus of S18, including Glu103, the proposed active site base, facilitating proton exchange and catalysis."xsd:string
http://purl.uniprot.org/citations/18596200http://purl.org/dc/terms/identifier"doi:10.1110/ps.035899.108"xsd:string
http://purl.uniprot.org/citations/18596200http://purl.org/dc/terms/identifier"doi:10.1110/ps.035899.108"xsd:string
http://purl.uniprot.org/citations/18596200http://purl.org/dc/terms/identifier"doi:10.1110/ps.035899.108"xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/author"Blanchard J.S."xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/author"Blanchard J.S."xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/author"Vetting M.W."xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/author"Vetting M.W."xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/author"Yu M."xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/author"Yu M."xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/author"Bareich D.C."xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/author"Bareich D.C."xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/name"Protein Sci."xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/name"Protein Sci."xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/pages"1781-1790"xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/pages"1781-1790"xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/title"Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT responsible for N(alpha)-acetylation of ribosomal protein S18."xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/title"Crystal structure of RimI from Salmonella typhimurium LT2, the GNAT responsible for N(alpha)-acetylation of ribosomal protein S18."xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/18596200http://purl.uniprot.org/core/volume"17"xsd:string