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    The Hemophore HasA from Yersinia pestis (HasAyp) Coordinates Hemin with a Single Residue, Tyr75, and with Minimal Conformational Change

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    Kumar_ACS_2013.pdf (1.109Mb)
    Issue Date
    2013-04-23
    Author
    Kumar, Ritesh
    Lovell, Scott
    Matsumura, Hirotoshi
    Battaile, Kevin P.
    Moënne-Loccoz, Pierre
    Rivera, Mario
    Publisher
    ACS
    Type
    Article
    Article Version
    Scholarly/refereed, author accepted manuscript
    Rights
    Copyright © 2013 American Chemical Society
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    Abstract
    Hemophores from Serratia marcescens (HasAsm) and Pseudomonas aeruginosa (HasAp) bind hemin between two loops, which harbor the axial ligands H32 and Y75. Hemin binding to the Y75 loop triggers closing of the H32 loop and enables binding of H32. Because Yersinia pestis HasA (HasAyp) presents a Gln at position 32, we determined the structures of apo-and holo-HasAyp. Surprisingly, the Q32 loop in apo-HasAyp is already in the closed conformation but no residue from the Q32 loop binds hemin in holo-HasAyp. In agreement with the minimal reorganization between the apo-and holo-structures, the hemin on-rate is too fast to detect by conventional stopped-flow measurements.
    URI
    http://hdl.handle.net/1808/23752
    DOI
    https://doi.org/10.1021/bi400280z
    Collections
    • Molecular Biosciences Scholarly Works [531]
    Citation
    Kumar, R., Lovell, S., Matsumura, H., Battaile, K. P., Moënne-Loccoz, P., & Rivera, M. (2013). The Hemophore HasA from Yersinia pestis (HasAyp) Coordinates Hemin with a Single Residue, Tyr75, and with Minimal Conformational Change. Biochemistry, 52(16), 2705–2707. http://doi.org/10.1021/bi400280z

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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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