1v96
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(New page: 200px<br /><applet load="1v96" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v96, resolution 1.75Å" /> '''Crystal structure of...)
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Revision as of 19:45, 24 November 2007
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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
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