2CZW

Crystal structure analysis of protein component Ph1496p of P.horikoshii ribonuclease P

2CZW の概要

• エントリーDOI: 10.2210/pdb2czw/pdb
• 関連するPDBエントリー: 1PXW
• 分子名称: 50S ribosomal protein L7Ae (2 entities in total)
• 機能のキーワード: ribonuclease p, ribonucleoprotein, ribosome, hydrolase
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13573.87

構造登録者

Fukuhara, H.,Kifusa, M.,Watanabe, M.,Terada, A.,Honda, T.,Numata, T.,Kakuta, Y.,Kimura, M. (登録日: 2005-07-19, 公開日: 2006-04-25, 最終更新日: 2024-03-13)

主引用文献

Fukuhara, H.,Kifusa, M.,Watanabe, M.,Terada, A.,Honda, T.,Numata, T.,Kakuta, Y.,Kimura, M.
A fifth protein subunit Ph1496p elevates the optimum temperature for the ribonuclease P activity from Pyrococcus horikoshii OT3
Biochem.Biophys.Res.Commun., 343:956-964, 2006

PubMed Abstract: Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of the 5' leader sequence of precursor tRNA. We previously found that the reconstituted particle (RP) composed of RNase P RNA and four proteins (Ph1481p, Ph1601p, Ph1771p, and Ph1877p) in the hyperthermophilic archaeon Pyrococcus horikoshii OT3 exhibited the RNase P activity, but had a lower optimal temperature (around at 55 degrees C), as compared with 70 degrees C of the authentic RNase P from P. horikoshii [Kouzuma et al., Biochem. Biophys. Res. Commun. 306 (2003) 666-673]. In the present study, we found that addition of a fifth protein Ph1496p, a putative ribosomal protein L7Ae, to RP specifically elevated the optimum temperature to about 70 degrees C comparable to that of the authentic RNase P. Characterization using gel shift assay and chemical probing localized Ph1496p binding sites on two stem-loop structures encompassing nucleotides A116-G201 and G229-C276 in P. horikoshii RNase P RNA. Moreover, the crystal structure of Ph1496p was determined at 2.0 A resolution by the molecular replacement method using ribosomal protein L7Ae from Haloarcula marismortui as a search model. Ph1496p comprises five alpha-helices and a four stranded beta-sheet. The beta-sheet is sandwiched by three helices (alpha1, alpha4, and alpha5) at one side and two helices (alpha2 and alpha3) at other side. The archaeal ribosomal protein L7Ae is known to be a triple functional protein, serving as a protein component in ribosome and ribonucleoprotein complexes, box C/D, and box H/ACA. Although we have at present no direct evidence that Ph1496p is a real protein component in the P. horikoshii RNase P, the present result may assign an RNase P protein to L7Ae as a fourth function.

PubMed: 16574071
DOI: 10.1016/j.bbrc.2006.02.192

実験手法

X-RAY DIFFRACTION (1.9 Å)