1V76

Crystal Structure of Archaeal Ribonuclease P Protein Ph1771p from Pyrococcus horikoshii OT3

1V76 の概要

• エントリーDOI: 10.2210/pdb1v76/pdb
• 関連するPDBエントリー: 1PC0
• 分子名称: RNase P protein Ph1771p, SULFATE ION (3 entities in total)
• 機能のキーワード: rna binding protein, archaeal rnase p protein
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22584.42

構造登録者

Numata, T.,Kakuta, Y.,Kimura, M. (登録日: 2003-12-12, 公開日: 2004-10-05, 最終更新日: 2023-12-27)

主引用文献

Numata, T.,Ishimatsu, I.,Kakuta, Y.,Tanaka, I.,Kimura, M.
Crystal structure of archaeal ribonuclease P protein Ph1771p from Pyrococcus horikoshii OT3: an archaeal homolog of eukaryotic ribonuclease P protein Rpp29
Rna, 10:1423-1432, 2004

PubMed Abstract: Ribonuclease P (RNase P) is the endonuclease responsible for the removal of 5' leader sequences from tRNA precursors. The crystal structure of an archaeal RNase P protein, Ph1771p (residues 36-127) from hyperthermophilic archaeon Pyrococcus horikoshii OT3 was determined at 2.0 A resolution by X-ray crystallography. The structure is composed of four helices (alpha1-alpha4) and a six-stranded antiparallel beta-sheet (beta1-beta6) with a protruding beta-strand (beta7) at the C-terminal region. The strand beta7 forms an antiparallel beta-sheet by interacting with strand beta4 in a symmetry-related molecule, suggesting that strands beta4 and beta7 could be involved in protein-protein interactions with other RNase P proteins. Structural comparison showed that the beta-barrel structure of Ph1771p has a topological resemblance to those of Staphylococcus aureus translational regulator Hfq and Haloarcula marismortui ribosomal protein L21E, suggesting that these RNA binding proteins have a common ancestor and then diverged to specifically bind to their cognate RNAs. The structure analysis as well as structural comparison suggested two possible RNA binding sites in Ph1771p, one being a concave surface formed by terminal alpha-helices (alpha1-alpha4) and beta-strand beta6, where positively charged residues are clustered. A second possible RNA binding site is at a loop region connecting strands beta2 and beta3, where conserved hydrophilic residues are exposed to the solvent and interact specifically with sulfate ion. These two potential sites for RNA binding are located in close proximity. The crystal structure of Ph1771p provides insight into the structure and function relationships of archaeal and eukaryotic RNase P.

PubMed: 15317976
DOI: 10.1261/rna.7560904

実験手法

X-RAY DIFFRACTION (2 Å)