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    NMR characterization of the Type III Secretion System Tip Chaperone Protein PcrG of Pseudomonas aeruginosa

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    Chaudhury_ACS_2015.pdf (3.349Mb)
    Issue Date
    2015-11-03
    Author
    Chaudhury, Sukanya
    Nordhues, Bryce Andrew
    Kaur, Kawaljit
    Zhang, Na
    De Guzman, Roberto N.
    Publisher
    Biochemistry
    Type
    Article
    Article Version
    Scholarly/refereed, author accepted manuscript
    Rights
    Electronic version of an article published as Biochemistry, 54, 43, 2015, pp 6576-6585 10.1021/acs.biochem.5b00664 © World Scientific Publishing Company
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    Abstract
    Lung infection with Pseudomonas aeruginosa is the leading cause of death among cystic fibrosis patients. To initiate infection, P. aeruginosa assembles a protein nanomachine, the type III secretion system (T3SS) to inject bacterial proteins directly into target host cells. An important regulator of the P. aeruginosa T3SS is the chaperone protein PcrG, which forms a complex with the tip protein, PcrV. In addition to its role as a chaperone to the tip protein, PcrG also regulates protein secretion. PcrG homologs are also important in the T3SS of other pathogens such as Yersinia pestis, the causative agent of bubonic plague. The atomic structure of PcrG or any member of the family of tip protein chaperones is currently unknown. Here, we show by CD and NMR spectroscopy that PcrG lacks a tertiary structure. However, it is not completely disordered but contains secondary structures dominated by two long α-helices from residues 16–41 and 55–76. NMR backbone dynamics data show that the helices in PcrG have semi-rigid flexibility and they tumble as a single entity with similar backbone dynamics. NMR titrations show that the entire length of PcrG residues from 9–76 is involved in binding to PcrV. Thus the PcrG family of T3SS chaperone proteins is essentially partially folded.
    URI
    http://hdl.handle.net/1808/23228
    DOI
    https://doi.org/10.1021/acs.biochem.5b00664
    Collections
    • Molecular Biosciences Scholarly Works [528]
    Citation
    Chaudhury, S., Nordhues, B. A., Kaur, K., Zhang, N., & De Guzman, R. N. (2015). NMR characterization of the Type III Secretion System Tip Chaperone Protein PcrG of Pseudomonas aeruginosa. Biochemistry, 54(43), 6576–6585. http://doi.org/10.1021/acs.biochem.5b00664

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    Contact KU ScholarWorks
    785-864-8983
    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    785-864-8983

    KU Libraries
    1425 Jayhawk Blvd
    Lawrence, KS 66045
    Image Credits
     

     

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