Crystallization and preliminary X-ray crystallographic studies of the small form of glucose-inhibited division protein A from Thermus thermophilus HB8.
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 P3(1)21 or P3(2)21, with unit-cell parameters a = b = 78.51, c = 66.10 A and one monomer per asymmetric unit. The crystals were found to diffract X-rays to beyond 1.65 A resolution.
RIKEN Harima Institute/SPring-8, Koto 1-1-1, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan.
Wakana
W
Iwasaki
Hideyuki
H
Miyatake
Akio
A
Ebihara
Kunio
K
Miki
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D005947:Glucose / Q000378:metabolism; D008969:Molecular Sequence Data; D012343:RNA, Transfer / Q000378:metabolism; D016415:Sequence Alignment; D016963:Thermus thermophilus / Q000201:enzymology*; D013891:Thiouridine / Q000031:analogs & derivatives / Q000378:metabolism
D001426:Bacterial Proteins; D013891:Thiouridine; D012343:RNA, Transfer; D005947:Glucose