1PC0

NMR Structure of the Archaeal Homologue of RNase P Protein Rpp29

1PC0 の概要

• エントリーDOI: 10.2210/pdb1pc0/pdb
• 分子名称: Hypothetical protein AF1917 (1 entity in total)
• 機能のキーワード: sandwich, beta-sheet, rna binding protein
• 由来する生物種: Archaeoglobus fulgidus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6900.12

構造登録者

Sidote, D.J.,Hoffman, D.W. (登録日: 2003-05-15, 公開日: 2003-12-09, 最終更新日: 2024-05-22)

主引用文献

Sidote, D.J.,Hoffman, D.W.
NMR Structure of an Archaeal Homologue of Ribonuclease P Protein Rpp29
Biochemistry, 42:13541-13550, 2003

PubMed Abstract: A protein component of the Archaeoglobus fulgidus RNase P was expressed in Escherichia coli, purified, and structurally characterized using multidimensional NMR methods. The dominant structural feature of this 11 kDa protein is a sheet of six antiparallel beta-strands, wrapped around a core of conserved hydrophobic amino acids. Amide proton exchange and (15)N relaxation rate data provide evidence that the first 16 residues of the protein, located before the start of the first beta-strand, and the last 24 residues, located past the end of the last beta-strand, are relatively flexible; this contrasts with the relatively rigid and well-defined structure of the beta-sheet. Amino acid sequence comparisons among a diverse set of species indicate that the A. fulgidus protein is homologous to the human RNase P protein Rpp29, yeast RNase P protein Pop4, and a known archaeal RNase P protein from Methanobacter thermoautotrophicus; conserved hydrophobic residues indicate that the homologous protein in each of these species contains a similar beta-sheet structure. Conserved surface residues located in the loop connecting strands beta2 and beta3, the loop connecting strands beta4 and beta5, and in the flexible N- and C-terminal tails are most likely to have specific interactions with the RNA and other proteins of RNase P. The structural model of an RNase P protein component provided by the present work provides an essential step toward eventually understanding the overall architecture of this complex enzyme and the mechanism by which it performs its functions.

PubMed: 14622001
DOI: 10.1021/bi030170z

実験手法

SOLUTION NMR