Preliminary X-ray crystallographic analysis of tRNA pseudouridine 55 synthase from the thermophilic eubacterium Thermotoga maritima.
Thermotoga maritima TruB, an enzyme responsible for the formation of pseudouridine in tRNA, has been purified and crystallized by the hanging-drop vapour-diffusion method in 100 mM citrate pH 3.5, 200 mM Li(2)SO(4), 20% glycerol, 13% PEG 8000. Crystals display orthorhombic symmetry, with unit-cell parameters a = 47.39, b = 83.88, c = 98.72 A, and diffract to 2.0 A resolution using synchrotron radiation. A solution was obtained by molecular replacement using part of the recently published crystal structure of Escherichia coli TruB bound to a synthetic RNA.
Wouters
Johan
J
Institut de Recherches Microbiologiques JM Wiame, Belgium. jwouters@dbm.ulb.ac.be
Tricot
Catherine
C
Durbecq
Virginie
V
Roovers
Martine
M
Stalon
Victor
V
Droogmans
Louis
L
D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D019753:Intramolecular Lyases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D019751:Intramolecular Transferases; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D020124:Thermotoga maritima / Q000201:enzymology* / Q000235:genetics
D011994:Recombinant Proteins; D019751:Intramolecular Transferases; C096995:pseudouridine synthases; D019753:Intramolecular Lyases