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- Title
Purification, crystallization and X-ray crystallographic analysis of a putative exopolyphosphatase from Zymomonas mobilis.
- Authors
Zhang, Aili; Guo, Erhong; Qian, Lanfang; Bartlam, Mark; Tang, Nga-Yeung; Watt, Rory M.
- Abstract
Exopolyphosphatase (PPX) enzymes degrade inorganic polyphosphate (poly-P), which is essential for the survival of microbial cells in response to external stresses. In this study, a putative exopolyphosphatase from Zymomonas mobilis (ZmPPX) was crystallized. Crystals of the wild-type enzyme diffracted to 3.3 Å resolution and could not be optimized further. The truncation of 29 amino acids from the N-terminus resulted in crystals that diffracted to 1.8 Å resolution. The crystals belonged to space group C2, with unit-cell parameters a = 122.0, b = 47.1, c = 89.5 Å, α = γ = 90, β = 124.5°. An active-site mutant that crystallized in the same space group and with similar unit-cell parameters diffracted to 1.56 Å resolution. One molecule was identified per asymmetric unit. Analytical ultracentrifugation confirmed that ZmPPX forms a dimer in solution. It was confirmed that ZmPPX possesses exopolyphosphatase activity against a synthetic poly-P substrate.
- Subjects
EXOPOLYPHOSPHATASE; ZYMOMONAS mobilis; PROTEIN crystallography
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2016, Vol 72, Issue 3, p172
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X16000753