2av5
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Crystal structure of Pyrococcus furiosus Pop5, an archaeal Ribonuclease P protein
OverviewOverview
We have used NMR spectroscopy and x-ray crystallography to determine the, three-dimensional structure of PF1378 (Pfu Pop5), one of four protein, subunits of archaeal RNase P that shares a homolog in the eukaryotic, enzyme. RNase P is an essential and ubiquitous ribonucleoprotein enzyme, required for maturation of tRNA. In bacteria, the enzyme's RNA subunit is, responsible for cleaving the single-stranded 5' leader sequence of, precursor tRNA molecules (pre-tRNA), whereas the protein subunit assists, in substrate binding. Although in bacteria the RNase P holoenzyme consists, of one large catalytic RNA and one small protein subunit, in archaea and, eukarya the enzyme contains several (> or =4) protein subunits, each of, which lacks sequence similarity to the bacterial protein. The functional, role of the proteins is poorly understood, as is the increased complexity, in comparison to the bacterial enzyme. Pfu Pop5 has been directly, implicated in catalysis by the observation that it pairs with PF1914 (Pfu, Rpp30) to functionally reconstitute the catalytic domain of the RNA, subunit. The protein adopts an alpha-beta sandwich fold highly homologous, to the single-stranded RNA binding RRM domain. Furthermore, the, three-dimensional arrangement of Pfu Pop5's structural elements is, remarkably similar to that of the bacterial protein subunit. NMR spectra, have been used to map the interaction of Pop5 with Pfu Rpp30. The data, presented permit tantalizing hypotheses regarding the role of this protein, subunit shared by archaeal and eukaryotic RNase P.
About this StructureAbout this Structure
2AV5 is a Single protein structure of sequence from Pyrococcus furiosus. Active as Ribonuclease P, with EC number 3.1.26.5 Full crystallographic information is available from OCA.
ReferenceReference
Structure of Pfu Pop5, an archaeal RNase P protein., Wilson RC, Bohlen CJ, Foster MP, Bell CE, Proc Natl Acad Sci U S A. 2006 Jan 24;103(4):873-8. Epub 2006 Jan 17. PMID:16418270
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