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3D models of yeast RNase P/MRP proteins Rpp1p and Pop3p.

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.

SUBMITTER: Dlakic M

PROVIDER: S-EPMC1370701 | biostudies-literature | 2005 Feb

REPOSITORIES: biostudies-literature

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3D models of yeast RNase P/MRP proteins Rpp1p and Pop3p.

Dlakić Mensur M

RNA (New York, N.Y.) 20041221 2

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 ...[more]

PMID: 15613537

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