Structure of PIN-domain protein PH0500 from Pyrococcus horikoshii

Jeyaraman Jeyakanthan, Eiji Inagaki, Chizu Kuroishi, Tahir H. Tahirov

Research output: Contribution to journalArticle

15 Citations (Scopus)

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 Å 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 Å resolution to an R factor of 20.9% and the structure of PH0500-II has been refined at 2.0 Å 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.

Original languageEnglish (US)
Pages (from-to)463-468
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number5
DOIs
StatePublished - Dec 1 2005

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Pyrococcus horikoshii
R Factors
proteins
Pyrococcus
RNA Editing
Exonucleases
Protein Databases
Proteins
Archaea
Crystals
Amino Acid Sequence
crystals
editing
DNA
Dimers
amino acids
Protein Domains
deoxyribonucleic acid
dimers
RNA

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

Cite this

Structure of PIN-domain protein PH0500 from Pyrococcus horikoshii. / Jeyakanthan, Jeyaraman; Inagaki, Eiji; Kuroishi, Chizu; Tahirov, Tahir H.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 61, No. 5, 01.12.2005, p. 463-468.

Research output: Contribution to journalArticle

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