| Literature DB >> 24915085 |
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
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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