Structure of PIN-domain protein PH0500 from Pyrococcus horikoshii

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Jeyaraman JeyakanthanTahir H Tahirov

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.

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Citations

Oct 19, 2007·Proceedings of the National Academy of Sciences of the United States of America·Hong-Wei WangAilong Ke
Aug 27, 2009·Proceedings of the National Academy of Sciences of the United States of America·Allison C Lamanna, Katrin Karbstein
Feb 23, 2012·The Journal of Biological Chemistry·Jared D SharpNancy A Woychik
Jul 6, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Daijiro TakeshitaMasaru Tanokura
Jun 9, 2007·Proteins·Daijiro TakeshitaMasaru Tanokura
Dec 3, 2014·Biochemical and Biophysical Research Communications·Shuxia PengQuansheng Liu
Feb 9, 2017·Journal of Structural Biology·Kaushik HattiMathur R N Murthy
May 17, 2017·Protein Science : a Publication of the Protein Society·M SenissarD E Brodersen
Nov 24, 2020·Journal of Biomolecular Structure & Dynamics·Mathimaran AmalaJeyaraman Jeyakanthan

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