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Showing 1–4 of 4 results
Advanced filters: Author: Takamasa Teramoto Clear advanced filters

  • The post-translational protein modification tyrosine sulfation is catalysed by tyrosylprotein sulfotransferase (TPST). Teramoto et al. present the first crystal structure of the human TPST isoform 2 complexed with a substrate peptide derived from complement C4 and 3′phosphoadenosine-5′-phosphate, revealing the molecular basis of catalysis.

    • Takamasa Teramoto
    • Yukari Fujikawa
    • Yoshimitsu Kakuta
    Research
    Nature Communications
    Volume: 4, P: 1-9

  • Transfer RNA maturation requires removal of extra sequences for proper function. Here, authors reveal how HARP, a protein-based enzyme, forms dodecamers that recognize specific tRNA features and process both 5′-leader and 3′-trailer sequences, demonstrating functional evolution.

    • Takamasa Teramoto
    • Takeshi Koyasu
    • Yoshimitsu Kakuta
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-15

  • Takuo Minato and colleagues determine the crystal and cryo-EM structures of the native C-phycocyanin (CPC) from the thermophilic cyanobacterium, Thermoleptolyngbya sp. O77, which was found to adopt both a conventional hexameric structure and a novel octameric assembly. These findings provide new insights into the assembly of CPCs and their mechanism of energy transfer.

    • Takuo Minato
    • Takamasa Teramoto
    • Ki-Seok Yoon
    ResearchOpen Access
    Communications Biology
    Volume: 4, P: 1-10