4.0 Article

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

Publisher

INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X18007689

Keywords

RimK; poly-alpha-L-glutamate synthetase; structural polymorphism; Escherichia coli

Funding

  1. Waseda Research Institute for Science and Engineering
  2. Early Bird Program of the Waseda Research Institute for Science and Engineering

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Bacterial RimK is an enzyme that catalyzes the polyglutamylation of the C-terminus of ribosomal protein S6 and the synthesis of poly-alpha-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 angstrom 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-alpha-L-glutamate peptides and the polyglutamylation of ribosomal protein S6.

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