1v96 | pdb_00001v96
Crystal structure of hypothetical protein of unknown function from pyrococcus horikoshii OT3
|
Overview
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.
About this Structure
1V96 is a Single protein structure of sequence from Pyrococcus horikoshii with GOL as ligand. Full crystallographic information is available from OCA.
Reference
Structure of PIN-domain protein PH0500 from Pyrococcus horikoshii., Jeyakanthan J, Inagaki E, Kuroishi C, Tahirov TH, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt, 5):463-8. Epub 2005 Apr 26. PMID:16511069
Page seeded by OCA on Sat Nov 24 21:53:27 2007
