Structure of the RNase PH hexamer
RNase PH is a 3'-5' exoribonuclease and nucleotidyltransferase, present in archaea and bacteria, that is involved in tRNA processing. Contrary to hydrolytic enzymes, it is a phosphorolytic enzyme, meaning that it uses inorganic phosphate as a reactant to cleave nucleotide-nucleotide bonds, releasing diphosphate nucleotides. The active structure of the proteins is a homohexameric complex, consisting of three ribonuclease (RNase) PH dimers. RNase PH has homologues in many other organisms, which are referred to as RNase PH-like proteins. The part of another larger protein with a domain that is very similar to RNase PH is called an RNase PH domain (RPD).
Two highly related exoribonuclease complexes:
- Ishii; Nureki, O; Yokoyama, S; et al. (2003). "Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus". J Biol Chem. 278 (34): 32397–404. PMID 12746447. doi:10.1074/jbc.M300639200.
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