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

Nature Structural & Molecular Biology volume 18, pages 227–229 (2011)Cite this article

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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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Figure 1: The structure of XMRV protease.
Figure 2: Dimer interface regions in aspartic proteases.

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Acknowledgements

We acknowledge the use of beamline 22-ID of the Southeast Regional Collaborative Access Team (SER-CAT), located at the Advanced Photon Source (APS), Argonne National Laboratory. Use of the APS was supported by the US Department of Energy, Office of Science, Office of Basic Energy Sciences, under contract no. W-31-109-Eng-38. This work was supported in part by the Intramural Research Program of the US National Institutes of Health, National Cancer Institute, Center for Cancer Research and with federal funds from the National Cancer Institute, National Institutes of Health, under contract HHSN261200800001E. The content of this publication does not necessarily reflect the views or policies of the Department of Health and Human Services, nor does the mention of trade names, commercial products or organizations imply endorsement by the US Government.

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Authors and Affiliations

  1. Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland, USA

    Mi Li, Dongwen Zhou, Alla Gustchina & Alexander Wlodawer

  2. Basic Research Program, SAIC-Frederick, Frederick, Maryland, USA

    Mi Li

  3. Department of Biochemistry, University of Washington, Seattle, Washington, USA

    Frank DiMaio & David Baker

  4. Macromolecular Assembly Structure and Cell Signaling Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, Maryland, USA

    Jacek Lubkowski

  5. Synchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Argonne National Laboratory, Argonne, Illinois, USA

    Zbigniew Dauter

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  1. Mi Li
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  2. Frank DiMaio
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  7. David Baker
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  8. Alexander Wlodawer
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Contributions

M.L. produced the protein and grew crystals; M.L. and Z.D. collected and processed crystallographic data; M.L., F.D.M., D.Z., A.G., J.L., and Z.D. performed calculations, structure refinement and analysis; D.B. and A.W. supervised the project. All authors discussed the results and participated in writing the manuscript.

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Correspondence to Alexander Wlodawer.

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The authors declare no competing financial interests.

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Supplementary Text and Figures

Supplementary Figures 1–7, Supplementary Tables 1 and 2, and Supplementary Methods (PDF 3481 kb)

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Li, M., DiMaio, F., Zhou, D. et al. Crystal structure of XMRV protease differs from the structures of other retropepsins. Nat Struct Mol Biol 18, 227–229 (2011). https://doi.org/10.1038/nsmb.1964

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