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1udn
From Proteopedia
| 1udn, resolution 2.30Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||||
| Gene: | RPH (Aquifex aeolicus) | ||||||||
| Activity: | tRNA nucleotidyltransferase, with EC number 2.7.7.56 | ||||||||
| Domains: | RNase_PH, rph, RNase_PH_C | ||||||||
| Related: | 1udo, 1udq, 1uds | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB, TOPSAN | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus
RNase PH is one of the exoribonucleases that catalyze the 3' end processing of tRNA in bacteria. RNase PH removes nucleotides following the CCA sequence of tRNA precursors by phosphorolysis and generates mature tRNAs with amino acid acceptor activity. In this study, we determined the crystal structure of Aquifex aeolicus RNase PH bound with a phosphate, a co-substrate, in the active site at 2.3-A resolution. RNase PH has the typical alpha/beta fold, which forms a hexameric ring structure as a trimer of dimers. This ring structure resembles that of the polynucleotide phosphorylase core domain homotrimer, another phosphorolytic exoribonuclease. Four amino acid residues, Arg-86, Gly-124, Thr-125, and Arg-126, of RNase PH are involved in the phosphate-binding site. Mutational analyses of these residues showed their importance in the phosphorolysis reaction. A docking model with the tRNA acceptor stem suggests how RNase PH accommodates substrate RNAs.
Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus., Ishii R, Nureki O, Yokoyama S, J Biol Chem. 2003 Aug 22;278(34):32397-404. Epub 2003 May 12. PMID:12746447
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1UDN is a 1 chain structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.
Reference
- Ishii R, Nureki O, Yokoyama S. Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus. J Biol Chem. 2003 Aug 22;278(34):32397-404. Epub 2003 May 12. PMID:12746447
Page seeded by OCA on Tue Feb 17 13:40:11 2009
