Structural analysis of a novel S-linked sugar transferase

2020 Fiscal Year Final Research Report

• Project/Area Number: 18K05340
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Review Section: Basic Section 37020:Chemistry and chemical methodology of biomolecules-related
• Research Institution: Gakushuin 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
• 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

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.

Free Research Field

構造生物学

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。