Crystallization and preliminary X-ray analysis of the tRNA thiolation enzyme MnmA from Escherichia coli complexed with tRNAGlu

Tomoyuki Numata, Yoshiho Ikeuchi, Shuya Fukai, Hiroaki Adachi, Hiroyoshi Matsumura, Kazufumi Takano, Satoshi Murakami, Tsuyoshi Inoue, Yusuke Mori, Takatomo Sasaki, Tsutomu Suzuki, Osamu Nureki

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23 Citations (Scopus)

Abstract

MnmA catalyzes a sulfuration reaction to synthesize 2-thiouridine at the wobble positions of tRNAGlu, tRNAGln and tRNA Lys in Escherichia coli. The binary complex of MnmA and tRNA Glu was crystallized in two different crystal forms: forms I and II. Cocrystallization of MnmA-tRNAGlu with ATP yielded form III crystals. The three crystal forms diffracted to 3.1, 3.4 and 3.4 Å resolution, respectively, using synchrotron radiation at SPring-8. These crystals belong to space groups C2, I212121 and C2, with unit-cell parameters a = 225.4, b = 175.8, c = 53.0 Å, β = 101.6°, a = 101.5, b = 108.0, c = 211.2 Å and a = 238.1, b = 102.1, c = 108.2 Å, β = 117.0°, respectively. The asymmetric units of these crystals are expected to contain two, one and two MnmA-tRNAGlu complexes, respectively.

Original languageEnglish
Pages (from-to)368-371
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume62
Issue number4
DOIs
Publication statusPublished - Apr 2006
Externally publishedYes

All Science Journal Classification (ASJC) codes

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

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