Crystal structure of a purine/pyrimidine phosphoribosyltransferase-related protein from Thermus thermophilus HB8

Peter H. Rehse, Tahir H. Tahirov

Research output: Contribution to journalArticle

5 Scopus citations

Abstract

Adenine phosphoribosyltransferase (APRTase) is a widely distributed enzyme involved in the salvage of adenine to form an adenine nucleotide. We crystallized and determined the X-ray crystallographic structure of a purine/pyrimidine phosphoribosyltransferase-related protein from the thermophilic bacterium, Thermus thermophilus HB8. The crystal space group was C2 with unit cell dimensions of a = 167.42 Å, b = 61.41 Å, c = 102.39 Å, β = 94.0°. Initial phases were determined to 2.6 Å using the multiple wavelength anomalous dispersion method and selenomethionine substituted protein (Se-MAD), and refined using a 1.9 Å "native" data set. The asymmetric unit contains two pairs of identical dinners, each related by noncrystallographic two-fold symmetry. The fifth monomer forms a similar dinner across a crystallographic two-fold axis. These dimers appear to be the biological unit with both monomers contributing to an unusual highly charged arginine-rich bridge region separating the two active sites. Comparison with distantly related APRTases reveal similarities and differences of the active site.

Original languageEnglish (US)
Pages (from-to)658-665
Number of pages8
JournalProteins: Structure, Function and Genetics
Volume61
Issue number3
DOIs
StatePublished - Nov 15 2005

Keywords

  • Adenosine phosphoribosyltransferase
  • X-ray

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology

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