Crystallization and preliminary X-ray crystallographic studies of the small form of glucose-inhibited division protein A from Thermus thermophilus HB8

Authors: Iwasaki, Wakana; Miyatake, Hideyuki; Ebihara, Akio; Miki, Kunio

Source: Acta Crystallographica Section D, Volume 60, Number 3, March 2004 , pp. 515-517(3)

Publisher: Blackwell Publishing

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Abstract:

Glucose-inhibited division protein A (GidA) acts in tRNA modification. It has been suggested that GidA is involved in the biosynthesis of the hypermodified nucleotide 5-methylaminomethyl-2-thiouridine in the wobble position of bacterial tRNAs, which stabilizes codon-anticodon interactions. Thermus thermophilus HB8 has a putative small gidA gene in addition to the normal gidA gene. The crystallization and preliminary X-ray crystallographic studies of the product of this small gidA gene (GidA_small) are reported here. The crystals belong to space group P3₁21 or P3₂21, with unit-cell parameters a = b = 78.51, c = 66.10 Å and one monomer per asymmetric unit. The crystals were found to diffract X-rays to beyond 1.65 Å resolution.

Keywords: glucose-inhibited division protein A; Thermus thermophilus

Document Type: Research article

DOI: 10.1107/S0907444904000721

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