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Structural analysis of a novel S-linked sugar transferase

Research Project

Project/Area Number 18K05340
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeMulti-year Fund
Section一般
Review Section Basic Section 37020:Chemistry and chemical methodology of biomolecules-related
Research InstitutionGakushuin University

Principal Investigator

Nakamura Akira  学習院大学, 理学部, 助教 (40432356)

Project Period (FY) 2018-04-01 – 2021-03-31
Project Status Completed (Fiscal Year 2020)
Budget Amount *help
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2020: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2019: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2018: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Keywords抗生物質 / ペプチド / 糖転移酵素 / 構造生物学 / 結晶構造解析 / X線結晶構造解析 / 糖転移反応 / S-結合型
Outline of Final Research Achievements

Protein glycosylation is one of the most common post-translational modifications. N-linked and O-linked glycosylation are the most abundant types, in which sugar is attached to the side chain of asparagine and serine/threonine residues, respectively. In addition, S-linked glycosylation on cysteine residues has been recently known. In this study, a bacterial S-linked glycosyltransferase involved in biosynthesis of a peptide antibiotic was focused on for the purpose of understanding the reaction mechanism of S-glycosylation by the glycosyltransferase, and the crystal structure of the enzyme was successfully determined.

Academic Significance and Societal Importance of the Research Achievements

本研究により、S-結合型糖転移酵素の立体構造が明らかとなり、他の糖転移酵素とは異なる構造的特徴も見出された。S-結合型糖は、構造的に類似したO-結合型糖よりも加水分解されにくいという特徴があるため、本研究成果により得られた知見をもとに、ペプチド性抗生物質へのS-結合型糖付加による新規抗生物質の開発や、チオール含有化合物への糖付加による物性変化といった研究に資するS-結合型糖転移酵素の酵素改変へと繋がることが期待される。

Report

(4 results)
  • 2020 Annual Research Report   Final Research Report ( PDF )
  • 2019 Research-status Report
  • 2018 Research-status Report
  • Research Products

    (6 results)

All 2021 2020 2019

All Journal Article (2 results) (of which Int'l Joint Research: 1 results,  Peer Reviewed: 2 results,  Open Access: 1 results) Presentation (4 results) (of which Invited: 1 results)

  • [Journal Article] Highlighting the potential utility of MBP crystallization chaperone for Arabidopsis BIL1/BZR1 transcription factor-DNA complex2021

    • Author(s)
      Nosaki Shohei、Terada Tohru、Nakamura Akira、Hirabayashi Kei、Xu Yuqun、Bui Thi Bao Chau、Nakano Takeshi、Tanokura Masaru、Miyakawa Takuya
    • Journal Title

      Scientific Reports

      Volume: 11 Issue: 1 Pages: 3879-3879

    • DOI

      10.1038/s41598-021-83532-2

    • Related Report
      2020 Annual Research Report
    • Peer Reviewed / Open Access / Int'l Joint Research
  • [Journal Article] Identification of novel interacting regions involving calcineurin and nuclear factor of activated T cells2020

    • Author(s)
      Kitamura Noriko、Shindo Mayumi、Ohtsuka Jun、Nakamura Akira、Tanokura Masaru、Hiroi Takachika、Kaminuma Osamu
    • Journal Title

      The FASEB Journal

      Volume: 34 Issue: 2 Pages: 3197-3208

    • DOI

      10.1096/fj.201902229

    • Related Report
      2019 Research-status Report
    • Peer Reviewed
  • [Presentation] 特徴的な化学結合を形成するペプチド性抗生物質の生合成酵素の構造解析2020

    • Author(s)
      中村 顕、松浦 辰信、深谷 翼、椎名 彩圭、関 友梨栄、関口 和樹、籾山 瑞季、小島 修一
    • Organizer
      日本生化学会
    • Related Report
      2020 Annual Research Report
    • Invited
  • [Presentation] プロセッシング前の状態の結晶構造に基づくSubtilisinの成熟過程の解析2019

    • Author(s)
      石田 航基, 西本 亜香音, 中村 顕, 小島 修一
    • Organizer
      日本生化学会
    • Related Report
      2019 Research-status Report
  • [Presentation] X線結晶構造解析に基づくSubtilisinにおける成熟過程の分析2019

    • Author(s)
      石田 航基, 西本 亜香音, 中村 顕, 小島 修一
    • Organizer
      日本結晶学会
    • Related Report
      2019 Research-status Report
  • [Presentation] リゾクチシン生合成酵素の結晶構造解析2019

    • Author(s)
      1.中村 顕, 松浦 辰信, 椎名 彩圭, 関 友梨栄, 関口 和樹, 籾山 瑞季, 小島 修一
    • Organizer
      日本結晶学会
    • Related Report
      2019 Research-status Report

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Published: 2018-04-23   Modified: 2022-01-27  

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