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標題: Structure and mechanism of an antibiotics-synthesizing 3-hydroxykynurenine C-methyltransferase
作者: Chen, Sheng-Chia
Huang, Chi-Hung
Lai, Shu-Jung
Liu, Jai-Shin
Fu, Pin-Kuei
Tseng, Shih-Ting
Yang, Chia Shin
Lai, Mei-Chin
Ko, Tzu-Ping
Chen, Yeh
關鍵字: Actinobacteria;Anti-Bacterial Agents;Bacterial Proteins;Binding Sites;Crystallography, X-Ray;Kynurenine;Ligands;Methyltransferases;Models, Molecular;Mutant Proteins;Protein Multimerization;Protein Structure, Secondary
Project: Scientific reports, Volume 5, Page(s) 10100.
Streptosporangium sibiricum SibL catalyzes the methyl transfer from S-adenosylmethionine (SAM) to 3-hydroxykynurenine (3-HK) to produce S-adenosylhomocysteine (SAH) and 3-hydroxy-4-methyl-kynurenine for sibiromycin biosynthesis. Here, we present the crystal structures of apo-form Ss-SibL, Ss-SibL/SAH binary complex and Ss-SibL/SAH/3-HK ternary complex. Ss-SibL is a homodimer. Each subunit comprises a helical N-terminal domain and a Rossmann-fold C-terminal domain. SAM (or SAH) binding alone results in domain movements, suggesting a two-step catalytic cycle. Analyses of the enzyme-ligand interactions and further mutant studies support a mechanism in which Tyr134 serves as the principal base in the transferase reaction of methyl group from SAM to 3-HK.
DOI: 10.1038/srep10100
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