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Updated: Jul 16, 2026
09:17
3D Printing of Biomolecular Models for Research and Pedagogy
Published on: March 13, 2017
3D models of yeast RNase P/MRP proteins Rpp1p and Pop3p
RNA (New York, N.Y.)
|December 23, 2004
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.
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