1QMI
Crystal structure of RNA 3'-terminal phosphate cyclase, an ubiquitous enzyme with unusual topology
Summary for 1QMI
| Entry DOI | 10.2210/pdb1qmi/pdb |
| Related | 1QMH |
| Descriptor | RNA 3'-TERMINAL PHOSPHATE CYCLASE (1 entity in total) |
| Functional Keywords | ligase, 2'3'cyclic phosphate rna |
| Biological source | ESCHERICHIA COLI |
| Cellular location | Cytoplasm: P46849 |
| Total number of polymer chains | 4 |
| Total formula weight | 148994.81 |
| Authors | Palm, G.J.,Billy, E.,Filipowicz, W.,Wlodawer, A. (deposition date: 1999-09-28, release date: 2000-01-11, Last modification date: 2013-04-17) |
| Primary citation | Palm, G.J.,Billy, E.,Filipowicz, W.,Wlodawer, A. Crystal Structure of RNA 3'-Terminal Phosphate Cyclase, a Ubiquitous Enzyme with Unusual Topology Structure, 8:13-, 2000 Cited by PubMed Abstract: RNA cyclases are a family of RNA-modifying enzymes that are conserved in eucarya, bacteria and archaea. They catalyze the ATP-dependent conversion of the 3'-phosphate to the 2',3'-cyclic phosphodiester at the end of RNA, in a reaction involving formation of the covalent AMP-cyclase intermediate. These enzymes might be responsible for production of the cyclic phosphate RNA ends that are known to be required by many RNA ligases in both prokaryotes and eukaryotes. PubMed: 10673421DOI: 10.1016/S0969-2126(00)00076-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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