1V96

Crystal structure of hypothetical protein of unknown function from pyrococcus horikoshii OT3

1V96 の概要

• エントリーDOI: 10.2210/pdb1v96/pdb
• 分子名称: hypothetical protein PH0500, GLYCEROL (3 entities in total)
• 機能のキーワード: rossmann fold, trna synthetase, nucleotide binding protein, structural genomics, riken structural genomics/proteomics initiative, rsgi, unknown function
• 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: 34696.82

構造登録者

Jeyakanthan, J.,Tahirov, T.H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2004-01-21, 公開日: 2005-02-01, 最終更新日: 2023-12-27)

主引用文献

Jeyakanthan, J.,Inagaki, E.,Kuroishi, C.,Tahirov, T.H.
Structure of PIN-domain protein PH0500 from Pyrococcus horikoshii.
Acta Crystallogr.,Sect.F, 61:463-468, 2005

PubMed Abstract: 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.

PubMed: 16511069
DOI: 10.1107/S1744309105012406

実験手法

X-RAY DIFFRACTION (1.75 Å)