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

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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)385-390
Number of pages6
JournalActa Crystallographica Section F: Structural Biology Communications
Volume74
Issue number7
DOIs
Publication statusPublished - 2018 Jul

Keywords

  • Escherichia coli
  • Poly-α-L-glutamate synthetase
  • RimK
  • Structural polymorphism

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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