Literature DB >> 24915085

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

Anna I Erickson1, Reta D Sarsam2, Andrew J Fisher1.   

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.

Entities:  

Keywords:  3′,5′-bisphosphate nucleotidase; 3′-phosphoadenosine 5′-phosphate; CysQ; Mycobacterium tuberculosis; PAP; Rv2131c; monophosphatase

Mesh:

Substances:

Year:  2014        PMID: 24915085      PMCID: PMC4051529          DOI: 10.1107/S2053230X14008619

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN: 2053-230X            Impact factor:   1.056


  14 in total

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10.  Rv2131c from Mycobacterium tuberculosis is a CysQ 3'-phosphoadenosine-5'-phosphatase.

Authors:  Stavroula K Hatzios; Anthony T Iavarone; Carolyn R Bertozzi
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