Jeyakanthan Jeyaraman, Inagaki Eiji, Kuroishi Chizu, Tahirov Tahir H
Advanced Protein Crystallography Research Group, RIKEN Harima Institute, 1-1-1 Kouto, Sayo-gun, Hyogo 679-5148, Japan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt 5):463-8. doi: 10.1107/S1744309105012406. Epub 2005 Apr 26.
The Pyrococcus horikoshii OT3 protein PH0500 is highly conserved within the Pyrococcus genus of hyperthermophilic archaea and shows low amino-acid sequence similarity with a family of PIN-domain proteins. The protein has been expressed, purified and crystallized in two crystal forms: PH0500-I and PH0500-II. The structure was determined at 2.0 A by the multiple anomalous dispersion method using a selenomethionyl derivative of crystal form PH0500-I (PH0500-I-Se). The structure of PH0500-I has been refined at 1.75 A resolution to an R factor of 20.9% and the structure of PH0500-II has been refined at 2.0 A resolution to an R factor of 23.4%. In both crystal forms as well as in solution the molecule appears to be a dimer. Searches of the databases for protein-fold similarities confirmed that the PH0500 protein is a PIN-domain protein with possible exonuclease activity and involvement in DNA or RNA editing.
嗜热栖热菌OT3蛋白PH0500在嗜热古菌的栖热菌属中高度保守,并且与PIN结构域蛋白家族的氨基酸序列相似性较低。该蛋白已被表达、纯化,并以两种晶体形式结晶:PH0500-I和PH0500-II。使用晶体形式PH0500-I(PH0500-I-Se)的硒代甲硫氨酸衍生物,通过多波长反常散射法在2.0 Å分辨率下确定了其结构。PH0500-I的结构已在1.75 Å分辨率下精修至R因子为20.9%,PH0500-II的结构已在2.0 Å分辨率下精修至R因子为23.4%。在两种晶体形式以及溶液中,该分子似乎都是二聚体。在数据库中搜索蛋白质折叠相似性证实,PH0500蛋白是一种具有可能的核酸外切酶活性并参与DNA或RNA编辑的PIN结构域蛋白。