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Visualizing molecular juggling within a B12-dependent methyltransferase complex

Author

Listed:
  • Yan Kung

    (Massachusetts Institute of Technology)

  • Nozomi Ando

    (Massachusetts Institute of Technology
    Howard Hughes Medical Institute, Massachusetts Institute of Technology)

  • Tzanko I. Doukov

    (Massachusetts Institute of Technology
    Present addresses: Stanford Synchrotron Radiation Lightsource, Menlo Park, California 94025, USA (T.I.D.); Institute of Marine and Environmental Technology, University of Maryland Center for Environmental Science, Baltimore, Maryland 21202, USA (L.C.B.).)

  • Leah C. Blasiak

    (Massachusetts Institute of Technology
    Present addresses: Stanford Synchrotron Radiation Lightsource, Menlo Park, California 94025, USA (T.I.D.); Institute of Marine and Environmental Technology, University of Maryland Center for Environmental Science, Baltimore, Maryland 21202, USA (L.C.B.).)

  • Güneş Bender

    (University of Michigan)

  • Javier Seravalli

    (University of Nebraska)

  • Stephen W. Ragsdale

    (University of Michigan)

  • Catherine L. Drennan

    (Massachusetts Institute of Technology
    Howard Hughes Medical Institute, Massachusetts Institute of Technology
    Massachusetts Institute of Technology)

Abstract

The first three-dimensional description of all the protein modules required for the activation, protection and catalytic steps of B12-dependent methyl transfer.

Suggested Citation

  • Yan Kung & Nozomi Ando & Tzanko I. Doukov & Leah C. Blasiak & Güneş Bender & Javier Seravalli & Stephen W. Ragsdale & Catherine L. Drennan, 2012. "Visualizing molecular juggling within a B12-dependent methyltransferase complex," Nature, Nature, vol. 484(7393), pages 265-269, April.
    • Handle: RePEc:nat:nature:v:484:y:2012:i:7393:d:10.1038_nature10916
    DOI: 10.1038/nature10916
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    Cited by:

    1. Johnny Mendoza & Meredith Purchal & Kazuhiro Yamada & Markos Koutmos, 2023. "Structure of full-length cobalamin-dependent methionine synthase and cofactor loading captured in crystallo," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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