2IS3
Crystal Structure of Escherichia coli RNase T
Summary for 2IS3
| Entry DOI | 10.2210/pdb2is3/pdb |
| Related | 2F96 |
| Descriptor | Ribonuclease T, SULFATE ION (2 entities in total) |
| Functional Keywords | rnase, ribonuclease, exoribonuclease, exonuclease, nuclease, hydrolase, stable rna maturation, trna end-turnover |
| Biological source | Escherichia coli K12 |
| Total number of polymer chains | 4 |
| Total formula weight | 96752.55 |
| Authors | Zuo, Y.,Wang, Y.,Malhotra, A. (deposition date: 2006-10-16, release date: 2007-04-24, Last modification date: 2024-10-30) |
| Primary citation | Zuo, Y.,Zheng, H.,Wang, Y.,Chruszcz, M.,Cymborowski, M.,Skarina, T.,Savchenko, A.,Malhotra, A.,Minor, W. Crystal Structure of RNase T, an Exoribonuclease Involved in tRNA Maturation and End Turnover. Structure, 15:417-428, 2007 Cited by PubMed Abstract: The 3' processing of most bacterial precursor tRNAs involves exonucleolytic trimming to yield a mature CCA end. This step is carried out by RNase T, a member of the large DEDD family of exonucleases. We report the crystal structures of RNase T from Escherichia coli and Pseudomonas aeruginosa, which show that this enzyme adopts an opposing dimeric arrangement, with the catalytic DEDD residues from one monomer closely juxtaposed with a large basic patch on the other monomer. This arrangement suggests that RNase T has to be dimeric for substrate specificity, and agrees very well with prior site-directed mutagenesis studies. The dimeric architecture of RNase T is very similar to the arrangement seen in oligoribonuclease, another bacterial DEDD family exoribonuclease. The catalytic residues in these two enzymes are organized very similarly to the catalytic domain of the third DEDD family exoribonuclease in E. coli, RNase D, which is monomeric. PubMed: 17437714DOI: 10.1016/j.str.2007.02.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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