X-ray structure of tRNA pseudouridine synthase TruD reveals an inserted domain with a novel fold.
Pseudouridine synthases catalyse the isomerisation of uridine to pseudouridine in structural RNA. The pseudouridine synthase TruD, that modifies U13 in tRNA, belongs to a recently identified and large family of pseudouridine synthases present in all kingdoms of life. We report here the crystal structure of Escherichia coli TruD at 2.0 A resolution. The structure reveals an overall V-shaped molecule with an RNA-binding cleft formed between two domains: a catalytic domain and an insertion domain. The catalytic domain has a fold similar to that of the catalytic domains of previously characterised pseudouridine synthases, whereas the insertion domain displays a novel fold.
Ericsson
Ulrika B
UB
Department of Biochemistry and Biophysics, Stockholm University, Roslagstullsbacken 15, SE-114 21 Stockholm, Sweden.
Nordlund
Pär
P
Hallberg
B Martin
BM
D000595:Amino Acid Sequence; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D004583:Electrons; D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins / Q000737:chemistry*; D019751:Intramolecular Transferases / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D012343:RNA, Transfer / Q000737:chemistry; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D029968:Escherichia coli Proteins; C474390:Pus7 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D012343:RNA, Transfer; D019751:Intramolecular Transferases; C487102:TruD protein, E coli; C023199:tRNA-pseudouridine synthase I