1VS3

Crystal Structure of the tRNA Pseudouridine Synthase TruA From Thermus thermophilus HB8

Summary for 1VS3

• Entry DOI: 10.2210/pdb1vs3/pdb
• Descriptor: tRNA pseudouridine synthase A (2 entities in total)
• Functional Keywords: trua, pseudouridine synthase, trna modification, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, isomerase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 55506.54

Authors

Dong, X.,Bessho, Y.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2006-06-28, release date: 2006-12-12, Last modification date: 2023-12-27)

Primary citation

Dong, X.,Bessho, Y.,Shibata, R.,Nishimoto, M.,Shirouzu, M.,Kuramitsu, S.,Yokoyama, S.
Crystal structure of tRNA pseudouridine synthase TruA from Thermus thermophilus HB8.
Rna Biol., 3:115-122, 2006

PubMed Abstract: The pseudouridine synthase (Psi 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 A resolution. TruA and the other (Psi 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.

PubMed: 17114947
DOI: 10.4161/rna.3.3.3286

Experimental method

X-RAY DIFFRACTION (2.25 Å)