Expression, purification and preliminary X-ray diffraction studies of the transcriptional factor PyrR from Bacillus halodurans

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Aug 1;64(Pt 8):692-6. doi: 10.1107/S1744309108018307. Epub 2008 Jul 5.

Abstract

The PyrR transcriptional regulator is widely distributed in bacteria. This RNA-binding protein is involved in the control of genes involved in pyrimidine biosynthesis, in which uridyl and guanyl nucleotides function as effectors. Here, the crystallization and preliminary X-ray diffraction analysis of two crystal forms of Bacillus halodurans PyrR are reported. One of the forms belongs to the monoclinic space group P2(1) with unit-cell parameters a = 59.7, b = 87.4, c = 72.1 A, beta = 104.4 degrees , while the other form belongs to the orthorhombic space group P22(1)2(1) with unit-cell parameters a = 72.7, b = 95.9, c = 177.1 A. Preliminary X-ray diffraction data analysis and molecular-replacement solution revealed the presence of four and six monomers per asymmetric unit; a crystallographic tetramer is formed in both forms.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacillus / chemistry*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Base Sequence
  • Chromatography, Gel
  • Cloning, Molecular
  • Crystallography, X-Ray
  • DNA Primers
  • Electrophoresis, Polyacrylamide Gel
  • Models, Molecular
  • Pentosyltransferases / chemistry*
  • Pentosyltransferases / genetics
  • Pentosyltransferases / isolation & purification
  • Protein Conformation
  • Repressor Proteins / chemistry*
  • Repressor Proteins / genetics
  • Repressor Proteins / isolation & purification

Substances

  • Bacterial Proteins
  • DNA Primers
  • Repressor Proteins
  • Pentosyltransferases
  • PyrR protein, bacteria