Expression, purification and preliminary crystallographic analysis of Mycobacterium tuberculosis CysQ, a phosphatase involved in sulfur metabolism

Anna I. Erickson, Reta D. Sarsam, Andrew J Fisher

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

CysQ is part of the sulfur-activation pathway that dephosphorylates 3′-phosphoadenosine 5′-monophosphate (PAP) to regenerate adenosine 5′-monophosphate (AMP) and free phosphate. PAP is the product of sulfate-transfer reactions from sulfotransferases that use the universal sulfate donor 3′-phosphoadenosine 5′-phosphosulfate (PAPS). In some organisms PAP is also the product of PAPS reductases that reduce sulfate from PAPS to sulfite. CysQ from Mycobacterium tuberculosis, which plays an important role in the biosynthesis of sulfated glycoconjugates, was successfully purified and crystallized in 24% PEG 1500, 20% glycerol. X-ray diffraction data were collected to 1.7 Å resolution using a synchrotron-radiation source. Crystals grew in the orthorhombic space group P212121, with unit-cell parameters a = 40.3, b = 57.9, c = 101.7 Å and with one monomer per asymmetric unit.

Original languageEnglish (US)
Pages (from-to)750-753
Number of pages4
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
Issue number6
DOIs
StatePublished - 2014

Keywords

  • 3′,5′-bisphosphate nucleotidase
  • 3′-phosphoadenosine 5′-phosphate
  • CysQ
  • monophosphatase
  • Mycobacterium tuberculosis
  • PAP
  • Rv2131c

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Genetics
  • Structural Biology
  • Condensed Matter Physics
  • Medicine(all)

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