1k8w | pdb_00001k8w
Crystal structure of the E. coli pseudouridine synthase TruB bound to a T stem-loop RNA
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Overview
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.
About this Structure
1K8W is a Single protein structure of sequence from Escherichia coli with SO4 as ligand. Active as Pseudouridylate synthase, with EC number 4.2.1.70 Full crystallographic information is available from OCA.
Reference
Cocrystal structure of a tRNA Psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme., Hoang C, Ferre-D'Amare AR, Cell. 2001 Dec 28;107(7):929-39. PMID:11779468
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