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: 10673421 DOI: 10.1016/S0969-2126(00)00076-9 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.8 Å)

Structure validation