Structural and biochemical analysis of a unique phosphatase from Bdellovibrio bacteriovorus reveals its structural and functional relationship with the protein tyrosine phosphatase class of phytase

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dc.contributor.authorGruninger, Robert J.
dc.contributor.authorThibault, John
dc.contributor.authorCapeness, Michael J.
dc.contributor.authorTill, Robert
dc.contributor.authorMosimann, Steven C.
dc.contributor.authorSockett, R. Elizabeth
dc.contributor.authorSelinger, L. Brent
dc.contributor.authorLovering, Andrew L.
dc.date.accessioned2016-12-21T18:08:15Z
dc.date.available2016-12-21T18:08:15Z
dc.date.issued2014
dc.descriptionSherpa Romeo green journal: open accessen_US
dc.description.abstractBdellovibrio bacteriovorus is an unusual d-proteobacterium that invades and preys on other Gram-negative bacteria and is of potential interest as a whole cell therapeutic against pathogens of man, animals and crops. PTPs (protein tyrosine phosphatases) are an important class of enzyme involved in desphosphorylating a variety of substrates, often with implications in cell signaling. The B. bacteriovorus open reading frame Bd1204 is predicted to encode a PTP of unknown function. Bd1204 is both structurally and mechanistically related to the PTP-like phytase (PTPLP) class of enzymes and possesses a number of unique properties not observed in any other PTPLPs characterized to date. Bd1204 does not display catalytic activity against some common protein tyrosine phosphatase substrates but is highly specific for hydrolysis of phosphomonoester bonds of inositol hexakisphosphate. The structure reveals that Bd1204 has the smallest and least electropositive active site of all characterized PTPLPs to date yet possesses a unique substrate specificity characterized by a strict preference for inositol hexakisphosphate. These two active site features are believed to be the most significant contributors to the specificity of phytate degrading enzymes. We speculate that Bd1204 may be involved in phosphate acquisition outside of prey.en_US
dc.description.peer-reviewYesen_US
dc.identifier.citationGruninger, R.J., Thibault, J., Capeness, M.J., Till, R., Mosimann, S. C., Sockett, R. E., ... & Lovering, A. L. (2014). Structural and biochemical analysis of a unique phosphatase from Bdellovibrio bacteriovorus reveals its structural and functional relationship with the protein tyrosine phosphatase class of phytase. PLoS ONE, 9(4), e94403. doi:10.1371/journal.pone.0094403en_US
dc.identifier.urihttps://hdl.handle.net/10133/4752
dc.language.isoen_USen_US
dc.publisherPublic Library of Scienceen_US
dc.publisher.departmentDepartment of Biological Sciencesen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionLethbridge Research and Development Centreen_US
dc.publisher.institutionUniversity of Nottinghamen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.institutionUniversity of Birminghamen_US
dc.subjectBdellovibrio bacteriovorusen_US
dc.subjectProtein tyrosine phosphatasesen_US
dc.subjectPhytaseen_US
dc.subjectPhosphataseen_US
dc.titleStructural and biochemical analysis of a unique phosphatase from Bdellovibrio bacteriovorus reveals its structural and functional relationship with the protein tyrosine phosphatase class of phytaseen_US
dc.typeArticleen_US
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