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

Mensur Dlakić | Zendy

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

Author(s) -

Mensur Dlakić

Publication year - 2004

Publication title -

rna

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.037

H-Index - 171

eISSN - 1469-9001

pISSN - 1355-8382

DOI - 10.1261/rna.7128905

Subject(s) - biology , rnase p , yeast , archaea , protein subunit , rnase mrp , rna , rnase ph , homologous chromosome , rna binding protein , biochemistry , genetics , microbiology and biotechnology , computational biology , bacteria , gene

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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