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Originally published In Press as doi:10.1074/jbc.M212353200 on February 4, 2003

J. Biol. Chem., Vol. 278, Issue 15, 13151-13158, April 11, 2003
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An NMR-based Model of the Ubiquitin-bound Human Ubiquitin Conjugation Complex Mms2·Ubc13
THE STRUCTURAL BASIS FOR LYSINE 63 CHAIN CATALYSIS*,

Sean McKennaDagger §, Trevor MoraesDagger , Landon Pastushok||, Christopher PtakDagger , Wei Xiao||**, Leo SpyracopoulosDagger Dagger Dagger §§, and Michael J. EllisonDagger Dagger Dagger ¶¶

From the Dagger  Department of Biochemistry and the Dagger Dagger  Institute for Biomolecular Design, University of Alberta, Edmonton, Alberta T6G 2H7 and the || Department of Microbiology and Immunology, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5, Canada

A heterodimer composed of the catalytically active ubiquitin-conjugating enzyme hUbc13 and its catalytically inactive paralogue, hMms2, forms the catalytic core for the synthesis of an alternative type of multiubiquitin chain where ubiquitin molecules are tandemly linked to one another through a Lys-63 isopeptide bond. This type of linkage, as opposed to the more typical Lys-48-linked chains, serves as a non-proteolytic marker of protein targets involved in error-free post-replicative DNA repair and NF-kappa B signal transduction. Using a two-dimensional 1H-15N NMR approach, we have mapped: 1) the interaction between the subunits of the human Ubc13·Mms2 heterodimer and 2) the interactions between each of the subunits or heterodimer with a non-covalently bound acceptor ubiquitin or a thiolester-linked donor ubiquitin. Using these NMR-derived constraints and an unbiased docking approach, we have assembled the four components of this catalytic complex into a three-dimensional model that agrees well with its catalytic function.

* This work was supported in part by research grants from the National Cancer Institute of Canada (to M. J. E.) and the Alberta Heritage Foundation for Medical Research (AHFMR) (to L. S.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The online version of this article (available at http://www.jbc.org) contains Supplemental Figs. 1 and 2.

§ A Natural Sciences and Engineering Research Council of Canada scholar.

A Canadian Institutes of Health Research (CIHR) scholar.

** Funded by CIHR (Grant MOP-53240).

§§ An AHFMR medical scholar. To whom correspondence may be addressed: Dept. of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada. Tel.: 780-492-2417; Fax: 780-492-0886; E-mail: leo.spyracopoulos@ualberta.ca.

¶¶ To whom correspondence may be addressed: Dept. of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada. Tel.: 780-492-6352; Fax: 780-492-0886; E-mail: mike.ellison@ualberta.ca.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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