RNase PH

RNase PH

protein
Name = Ribonuclease PH
caption = Structure of the RNase PH hexamer


width = 220
HGNCid =
Symbol = RNASEPH
AltSymbols =
EntrezGene =
OMIM =
RefSeq =
UniProt =
PDB =
ECnumber = 2.7.7.56
Chromosome =
Arm =
Band =
LocusSupplementaryData =

RNase PH is an 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 cofactor to cleave nucleotide-nucleotide bonds, releasing diphosphate nucleotides. The active structure of the proteins is actually a homohexameric complex, consisting of three RNase PH dimers. [cite journal
author= Ishii "et al."
title=Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus
journal=J Biol Chem.
volume=278
pages=32397–404
year=2003
pmid=12746447
doi=10.1074/jbc.M300639200] RNase PH has homologues in many other organisms, which are referred to as RNase PH-like proteins. When a part of another larger protein has a domain that is very similar to RNase PH, this is called an RNase PH domain (RPD).

See also

Two highly related exoribonuclease complexes:
* Polynucleotide Phosphorylase
* Exosome complex

References

External links

* [http://www.rcsb.org/pdb/explore.do?structureId=1UDN Crystal structure of "Aquifex aeolicus" RNase PH at the RCSB Protein Data Bank]


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