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Crystal structure of XMRV protease differs from the structures of other retropepsins

  1. Author:
    Li, M.
    DiMaio, F.
    Zhou, D. W.
    Gustchina, A.
    Lubkowski, J.
    Dauter, Z.
    Baker, D.
    Wlodawer, A.

  2. Author Address

    [Li, Mi; Zhou, Dongwen; Gustchina, Alla; Wlodawer, Alexander] NCI, Prot Struct Sect, Macromol Crystallog Lab, Frederick, MD 21701 USA. [Li, Mi] SAIC Frederick, Basic Res Program, Frederick, MD USA. [DiMaio, Frank; Baker, David] Univ Washington, Dept Biochem, Seattle, WA 98195 USA. [Lubkowski, Jacek] NCI, Macromol Assembly Struct & Cell Signaling Sect, Macromol Crystallog Lab, Frederick, MD 21701 USA. [Dauter, Zbigniew] NCI, Synchrotron Radiat Res Sect, Macromol Crystallog Lab, Argonne Natl Lab, Argonne, IL USA.;Wlodawer, A, NCI, Prot Struct Sect, Macromol Crystallog Lab, Frederick, MD 21701 USA.;wlodawer@nih.gov
    1. Year: 2011
    2. Date: Feb
  2. Journal: Nature Structural & Molecular Biology
    1. 18
    2. 2
    3. Pages: 227-229
  4. Type of Article: Article
  5. ISSN: 1545-9985
  1. Abstract:

    Using energy and density guided Rosetta refinement to improve molecular replacement, we determined the crystal structure of the protease encoded by xenotropic murine leukemia virus-related virus (XMRV). Despite overall similarity of XMRV protease to other retropepsins, the topology of its dimer interface more closely resembles those of the monomeric, pepsin-like enzymes. Thus, XMRV protease may represent a distinct branch of the aspartic protease family.

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External Sources

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  2. DOI: 10.1038/nsmb.1964
  3. View record in Web of Science®
  4. WOS: 000286969200017

Library Notes

  1. Fiscal Year: FY2010-2011
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