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  • Trehalose 6-phosphate phosphatases of Pseudomonas aeruginosa

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    Accepted Manuscript (AM)
    Author(s)
    Cross, Megan
    Biberacher, Sonja
    Park, Suk-Youl
    Rajan, Siji
    Korhonen, Pasi
    Gasser, Robin B
    Kim, Jeong-Sun
    Coster, Mark J
    Hofmann, Andreas
    Griffith University Author(s)
    Hofmann, Andreas
    Coster, Mark J.
    Cross, Megan O.
    Biberacher, Sonja M.
    Rajan, Siji
    Year published
    2018
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    Abstract
    The opportunistic bacterium Pseudomonas aeruginosa has been recognized as an important pathogen of clinical relevance and is a leading cause of hospital-acquired infections. The presence of a glycolytic enzyme in Pseudomonas, which is known to be inhibited by trehalose 6-phosphate (T6P) in other organisms, suggests that these bacteria may be vulnerable to the detrimental effects of intracellular T6P accumulation. In the present study, we explored the structural and functional properties of trehalose 6-phosphate phosphatase (TPP) in P. aeruginosa in support of future target-based drug discovery. A survey of genomes revealed ...
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    The opportunistic bacterium Pseudomonas aeruginosa has been recognized as an important pathogen of clinical relevance and is a leading cause of hospital-acquired infections. The presence of a glycolytic enzyme in Pseudomonas, which is known to be inhibited by trehalose 6-phosphate (T6P) in other organisms, suggests that these bacteria may be vulnerable to the detrimental effects of intracellular T6P accumulation. In the present study, we explored the structural and functional properties of trehalose 6-phosphate phosphatase (TPP) in P. aeruginosa in support of future target-based drug discovery. A survey of genomes revealed the existence of 2 TPP genes with either chromosomal or extrachromosomal location. Both TPPs were produced as recombinant proteins, and characterization of their enzymatic properties confirmed specific, magnesium-dependent catalytic hydrolysis of T6P. The 3-dimensional crystal structure of the chromosomal TPP revealed a protein dimer arising through β-sheet expansion of the individual monomers, which possess the overall fold of halo-acid dehydrogenases.—Cross, M., Biberacher, S., Park, S.-Y., Rajan, S., Korhonen, P., Gasser, R. B., Kim, J.-S., Coster, M. J., Hofmann, A. Trehalose 6-phosphate phosphatases of Pseudomonas aeruginosa.
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    Journal Title
    FASEB JOURNAL
    Volume
    32
    Issue
    10
    DOI
    https://doi.org/10.1096/fj.201800500R
    Copyright Statement
    © 2018 Federation of American Societies for Experimental Biology. This is the author-manuscript version of this paper. Reproduced in accordance with the copyright policy of the publisher. Please refer to the journal website for access to the definitive, published version.
    Subject
    Biochemistry and cell biology
    Zoology
    Medical physiology
    Publication URI
    http://hdl.handle.net/10072/382753
    Collection
    • Journal articles

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