Structural polymorphism of the Escherichia coli poly-α-L-glutamate synthetase RimK

Yasuhiro Arimura, Tomonori Kono*, Kuniki Kino, Hitoshi Kurumizaka

*この研究の対応する著者

研究成果: Article査読

抄録

Bacterial RimK is an enzyme that catalyzes the polyglutamylation of the C-terminus of ribosomal protein S6 and the synthesis of poly-α-l-glutamate peptides using l-glutamic acid. In the present study, the crystal structure of the Escherichia coli RimK protein complexed with the ATP analogue AMP-PNP was determined at 2.05 A - resolution. Two different conformations of RimK, closed and open forms, were observed in the crystals. The structural polymorphism revealed in this study provided important information to understand the mechanism by which RimK catalyzes the synthesis of poly-α- l-glutamate peptides and the polyglutamylation of ribosomal protein S6.

本文言語English
ページ(範囲)385-390
ページ数6
ジャーナルActa Crystallographica Section F: Structural Biology Communications
74
7
DOI
出版ステータスPublished - 2018 7

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 遺伝学
  • 凝縮系物理学

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