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Structure of PIN-domain protein PH0500 from Pyrococcus horikoshii.

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.

SUBMITTER: Jeyakanthan J

PROVIDER: S-EPMC1952296 | biostudies-literature | 2005 May

REPOSITORIES: biostudies-literature

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Structure of PIN-domain protein PH0500 from Pyrococcus horikoshii.

Jeyakanthan Jeyaraman J Inagaki Eiji E Kuroishi Chizu C Tahirov Tahir H TH

Acta crystallographica. Section F, Structural biology and crystallization communications 20050426 Pt 5

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 ...[more]

PMID: 16511069

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