ArticleActa crystallographica. Section F, Structural biology communications2014
Expression, purification and preliminary crystallographic analysis of Mycobacterium tuberculosis CysQ, a phosphatase involved in sulfur metabolism.
Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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.
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