1v96
From Proteopedia
(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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| - | [[Image:1v96.gif|left|200px]]<br /><applet load="1v96" size=" | + | [[Image:1v96.gif|left|200px]]<br /><applet load="1v96" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1v96, resolution 1.75Å" /> | caption="1v96, resolution 1.75Å" /> | ||
'''Crystal structure of hypothetical protein of unknown function from pyrococcus horikoshii OT3'''<br /> | '''Crystal structure of hypothetical protein of unknown function from pyrococcus horikoshii OT3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Pyrococcus horikoshii OT3 protein PH0500 is highly conserved within | + | 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== | ==About this Structure== | ||
| - | 1V96 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1V96 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V96 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of PIN-domain protein PH0500 from Pyrococcus horikoshii., Jeyakanthan J, Inagaki E, Kuroishi C, Tahirov TH, Acta | + | Structure of PIN-domain protein PH0500 from Pyrococcus horikoshii., Jeyakanthan J, Inagaki E, Kuroishi C, Tahirov TH, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt, 5):463-8. Epub 2005 Apr 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16511069 16511069] |
[[Category: Pyrococcus horikoshii]] | [[Category: Pyrococcus horikoshii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Jeyakanthan, J.]] | [[Category: Jeyakanthan, J.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
| - | [[Category: Tahirov, T | + | [[Category: Tahirov, T H.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: nucleotide binding protein]] | [[Category: nucleotide binding protein]] | ||
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[[Category: trna synthetase]] | [[Category: trna synthetase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:32:48 2008'' |
Revision as of 13:32, 21 February 2008
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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 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 Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt, 5):463-8. Epub 2005 Apr 26. PMID:16511069
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