2F96

2.1 A crystal structure of Pseudomonas aeruginosa rnase T (Ribonuclease T)

Summary for 2F96

• Entry DOI: 10.2210/pdb2f96/pdb
• Descriptor: Ribonuclease T, MAGNESIUM ION (3 entities in total)
• Functional Keywords: rnase, rnt, rnase t, ribonuclease t, trna hydrolase, sad, psi, mcsg, protein structure initiative, midwest center for structural genomics, structural genomics, hydrolase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 50208.75

Authors

Zheng, H.,Chruszcz, M.,Cymborowski, M.,Wang, Y.,Gorodichtchenskaia, E.,Skarina, T.,Guthrie, J.,Savchenko, A.,Edwards, A.,Joachimiak, A.,Minor, W.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2005-12-05, release date: 2006-02-14, Last modification date: 2024-11-20)

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

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: 17437714
DOI: 10.1016/j.str.2007.02.004

Experimental method

X-RAY DIFFRACTION (2.09 Å)