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Article: Purification, crystallization and X-ray crystallographic analysis of a putative exopolyphosphatase from Zymomonas mobilis

TitlePurification, crystallization and X-ray crystallographic analysis of a putative exopolyphosphatase from Zymomonas mobilis
Authors
Issue Date2016
PublisherInternational Union of Crystallography. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1111/%28ISSN%291744-3091
Citation
Acta Crystallographica Section F: Structural Biology and Crystallization Communications Online, 2016, v. 72 n. 3, p. 172-178 How to Cite?
AbstractExopolyphosphatase (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.
Persistent Identifierhttp://hdl.handle.net/10722/224877
ISSN
2014 Impact Factor: 0.524

 

DC FieldValueLanguage
dc.contributor.authorZhang, A-
dc.contributor.authorGuo, E-
dc.contributor.authorQian, L-
dc.contributor.authorTang, NY-
dc.contributor.authorWatt, RM-
dc.contributor.authorBartlam, M-
dc.date.accessioned2016-04-18T03:33:44Z-
dc.date.available2016-04-18T03:33:44Z-
dc.date.issued2016-
dc.identifier.citationActa Crystallographica Section F: Structural Biology and Crystallization Communications Online, 2016, v. 72 n. 3, p. 172-178-
dc.identifier.issn1744-3091-
dc.identifier.urihttp://hdl.handle.net/10722/224877-
dc.description.abstractExopolyphosphatase (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.-
dc.languageeng-
dc.publisherInternational Union of Crystallography. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1111/%28ISSN%291744-3091-
dc.relation.ispartofActa Crystallographica Section F: Structural Biology and Crystallization Communications Online-
dc.rightsThe definitive version is available at www.blackwell-synergy.com-
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.titlePurification, crystallization and X-ray crystallographic analysis of a putative exopolyphosphatase from Zymomonas mobilis-
dc.typeArticle-
dc.identifier.emailWatt, RM: rmwatt@hku.hk-
dc.identifier.authorityWatt, RM=rp00043-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1107/S2053230X16000753-
dc.identifier.pmid26919520-
dc.identifier.hkuros257432-
dc.identifier.volume72-
dc.identifier.issue3-
dc.identifier.spage172-
dc.identifier.epage178-
dc.publisher.placeUnited States-

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