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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Date
2014
Authors
Gruninger, Robert J.
Thibault, John
Capeness, Michael J.
Till, Robert
Mosimann, Steven C.
Sockett, R. Elizabeth
Selinger, L. Brent
Lovering, Andrew L.
Journal Title
Journal ISSN
Volume Title
Publisher
Public Library of Science
Abstract
Bdellovibrio 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.
Description
Sherpa Romeo green journal: open access
Keywords
Bdellovibrio bacteriovorus , Protein tyrosine phosphatases , Phytase , Phosphatase
Citation
Gruninger, 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.0094403