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Research Paper
Crystal Structure of the tRNA Pseudouridine Synthase TruA from Thermus Thermophilus HB8
Xuesong Dong, Yoshitaka Bessho, Rie Shibata, Madoka Nishimoto, Mikako Shirouzu, Seiki Kuramitsu and Shigeyuki Yokoyama
volume 3 | issue 3
july/august/september 2006Pages: 115 - 121
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The pseudouridine synthase (Ψ synthase) TruA catalyzes the conversion of uridine to pseudouridine at positions 38, 39, and/or 40 in the anticodon stem-loop (ASL) of tRNA. We have determined the crystal structure of TruA from Thermus thermophilus HB8 at 2.25 Å resolution. TruA and the other Ψ synthases have a completely conserved active site aspartate, which suggests that the members of this enzyme family share a common catalytic mechanism. The T. thermophilus TruA structure reveals the remarkably flexible structural features in the tRNA-binding cleft, which may be responsible for the primary tRNA interaction. In addition, the charged residues occupying the intermediate positions in the cleft may lead the tRNA to the active site for catalysis. Based on the TruB-tRNA complex structure, the T. thermophilus TruA structure reveals that the tRNA probably makes the melting base pairs move into the cleft, and suggests that a conformational change of the substrate tRNA is necessary to facilitate access to the active site aspartate residue, deep within the cleft.
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDF If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.