Dlakic M (2005) 3D models of yeast RNase P/MRP proteins Rpp1p and Pop3p. RNA 11(2):123-7
Abstract: Sensitive profile searches and fold recognition were used to predict the structures of two yeast RNase P/MRP proteins. Rpp1p, which is one of the subunits common to eukaryotes and archaea, is predicted to adopt the seven-stranded TIM-barrel fold found in PHP phosphoesterases. Pop3p, initially thought to be one of the RNase P/MRP subunits unique to yeast, has been assigned the L7Ae/L30e fold. This RNA-binding fold is also present in human RNase P subunit Rpp38, raising the possibility that Pop3p and Rpp38 are functional homologs.
|Status: Published||Type: Letter | Research Support, U.S. Gov't, P.H.S.||PubMed ID: 15613537|
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Number of different genes curated to this paper: 2
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