Open AccessCrystallization and preliminary X‐ray analysis of the tRNA thiolation enzyme MnmA from Escherichia coli complexed with tRNA Glu
Author(s) -
Numata Tomoyuki,
Ikeuchi Yoshiho,
Fukai Shuya,
Adachi Hiroaki,
Matsumura Hiroyoshi,
Inoue Tsuyoshi,
Mori Yusuke,
Takano Kazufumi,
Sasaki Takatomo,
Suzuki Tsutomu,
Murakami Satoshi,
Nureki Osamu
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910600738x
Subject(s) - transfer rna , wobble base pair , escherichia coli , crystallography , crystallization , angstrom , crystal structure , resolution (logic) , stereochemistry , x ray crystallography , enzyme , chemistry , rna , diffraction , biochemistry , physics , organic chemistry , artificial intelligence , computer science , optics , gene
MnmA catalyzes a sulfuration reaction to synthesize 2‐thiouridine at the wobble positions of tRNA Glu , tRNA Gln 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–tRNA Glu 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 C 2, I 2 1 2 1 2 1 and C 2, 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–tRNA Glu complexes, respectively.