1V77

Crystal structure of the PH1877 protein

1V77 の概要

• エントリーDOI: 10.2210/pdb1v77/pdb
• 分子名称: hypothetical protein PH1877 (2 entities in total)
• 機能のキーワード: rnase p protein, tim-barrel, rna binding protein
• 由来する生物種: Pyrococcus horikoshii
• 細胞内の位置: Cytoplasm : O59543
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24734.13

構造登録者

Takagi, H.,Numata, T.,Kakuta, Y.,Kimura, M. (登録日: 2003-12-12, 公開日: 2004-08-31, 最終更新日: 2023-12-27)

主引用文献

Takagi, H.,Watanabe, M.,Kakuta, Y.,Kamachi, R.,Numata, T.,Tanaka, I.,Kimura, M.
Crystal structure of the ribonuclease P protein Ph1877p from hyperthermophilic archaeon Pyrococcus horikoshii OT3
Biochem.Biophys.Res.Commun., 319:787-794, 2004

PubMed Abstract: Ribonuclease P (RNase P) is a ribonucleoprotein complex involved in the processing of pre-tRNA. Protein Ph1877p is one of essential components of the hyperthermophilic archaeon Pyrococcus horikoshii OT3 RNase P [Biochem. Biophys. Res. Commun. 306 (2003) 666]. The crystal structure of Ph1877p was determined at 1.8A by X-ray crystallography and refined to a crystallographic R factor of 22.96% (Rfree of 26.77%). Ph1877p forms a TIM barrel structure, consisting of ten alpha-helices and seven beta-strands, and has the closest similarity to the TIM barrel domain of Escherichia coli cytosine deaminase with a root-mean square deviation of 3.0A. The protein Ph1877p forms an oblate ellipsoid, approximate dimensions being 45Ax43Ax39A, and the electrostatic representation indicated the presence of several clusters of positively charged amino acids present on the molecular surface. We made use of site-directed mutagenesis to assess the role of twelve charged amino acids, Lys42, Arg68, Arg87, Arg90, Asp98, Arg107, His114, Lys123, Lys158, Arg176, Asp180, and Lys196 related to the RNase P activity. Individual mutations of Arg90, Arg107, Lys123, Arg176, and Lys196 by Ala resulted in reconstituted particles with reduced enzymatic activities (32-48%) as compared with that reconstituted RNase P by wild-type Ph1877p. The results presented here provide an initial step for definite understanding of how archaeal and eukaryotic RNase Ps mediate substrate recognition and process 5'-leader sequence of pre-tRNA.

PubMed: 15184052
DOI: 10.1016/j.bbrc.2004.05.055

実験手法

X-RAY DIFFRACTION (1.8 Å)