1K8W

Crystal structure of the E. coli pseudouridine synthase TruB bound to a T stem-loop RNA

Summary for 1K8W

• Entry DOI: 10.2210/pdb1k8w/pdb
• Descriptor: 5'-R(*GP*GP*CP*AP*AP*CP*GP*GP*UP*(FHU)P*CP*GP*AP*UP*CP*CP*CP*GP*UP*UP*GP*C)-3', tRNA Pseudouridine Synthase B, SULFATE ION, ... (4 entities in total)
• Functional Keywords: protein-rna complex, t stem-loop, trna, lyase-rna complex, lyase/rna
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 44661.39

Authors

Hoang, C.,Ferre-D'Amare, A.R. (deposition date: 2001-10-25, release date: 2001-12-31, Last modification date: 2024-02-07)

Primary citation

Hoang, C.,Ferre-D'Amare, A.R.
Cocrystal structure of a tRNA Psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme.
Cell(Cambridge,Mass.), 107:929-939, 2001

PubMed Abstract: Pseudouridine (Psi) synthases catalyze the isomerization of specific uridines in cellular RNAs to pseudouridines and may function as RNA chaperones. TruB is responsible for the Psi residue present in the T loops of virtually all tRNAs. The close homolog Cbf5/dyskerin is the catalytic subunit of box H/ACA snoRNPs. These carry out the pseudouridylation of eukaryotic rRNA and snRNAs. The 1.85 A resolution structure of TruB bound to RNA reveals that this enzyme recognizes the preformed three-dimensional structure of the T loop, primarily through shape complementarity. It accesses its substrate uridyl residue by flipping out the nucleotide and disrupts the tertiary structure of tRNA. Structural comparisons with TruB demonstrate that all Psi synthases are descended from a common molecular ancestor.

PubMed: 11779468
DOI: 10.1016/S0092-8674(01)00618-3

Experimental method

X-RAY DIFFRACTION (1.85 Å)