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J. Biol. Chem., Vol. 280, Issue 48, 40122-40129, December 2, 2005

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Small Ubiquitin-like Modifier (SUMO) Recognition of a SUMO Binding Motif

A REVERSAL OF THE BOUND ORIENTATION^*

Jing Song, Ziming Zhang, Weidong Hu, and Yuan Chen1

From the Division of Immunology and Graduate School of Biological Sciences, Beckman Research Institute of the City of Hope, Duarte, California 91010

Sumoylation has recently been identified as an important mechanism that regulates protein interactions and localization in essential cellular functions, such as gene transcription, subnuclear structure formation, viral infection, and cell cycle progression. A SUMO binding amino acid sequence motif (SBM), which recognizes the SUMO moiety of modified proteins in sumoylation-dependent cellular functions, has been consistently identified by several recent studies. To understand the mechanism of SUMO recognition by the SBM, we have solved the solution structure of SUMO-1 in complex with a peptide containing the SBM derived from the protein PIASX (KVDVIDLTIESSSDEEEDPPAKR). Surprisingly, the structure reveals that the bound orientation of the SBM can reverse depending on the sequence context. The structure also reveals a novel mechanism of recognizing target sequences by a ubiquitin-like module. Unlike ubiquitin binding motifs, which all form helices and bind to the main -sheet of ubiquitin, the SBM forms an extended structure that binds between the -helix and a -strand of SUMO-1. This study provides a clear mechanism of the SBM sequence variations and its recognition of the SUMO moiety in sumoylated proteins.

Received for publication, June 28, 2005 , and in revised form, September 6, 2005.

The atomic coordinates and structure factors (code 2ASQ) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work is supported by National Institutes of Health Grant CA94595 (to Y. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Division of Immunology, Beckman Research Institute of the City of Hope, 1450 East Duarte Rd., Duarte, CA 91010. Tel.: 626-930-5408; Fax: 626-301-8186; E-mail: ychen{at}coh.org.

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