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Expression, purification and preliminary crystallographic analysis of Mycobacterium tuberculosis CysQ, a phosphatase involved in sulfur metabolism
Author(s) -
Erickson Anna I.,
Sarsam Reta D.,
Fisher Andrew J.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14008619
Subject(s) - chemistry , biosynthesis , biochemistry , sulfation , sulfur , glycoconjugate , mycobacterium tuberculosis , pyridoxal , sulfur metabolism , stereochemistry , metabolism , crystallography , phosphate , enzyme , tuberculosis , organic chemistry , medicine , pathology
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 P 2 1 2 1 2 1 , with unit‐cell parameters a = 40.3, b = 57.9, c = 101.7 Å and with one monomer per asymmetric unit.