Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase

Cappadocia, Laurant; Pichler, A.; Lima, Christopher D.

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Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase

Cappadocia, L., Pichler, A., & Lima, C. D. (2015). Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase. Nature Structural & Molecular Biology, 22(12), 968-975.

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Item Permalink: https://hdl.handle.net/someHandle/test/escidoc:902497 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-99D0-7

Genre: Journal Article

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Creators:
Cappadocia, Laurant¹, Author
Pichler, A.², Author
Lima, Christopher D.^{1, 3}, Author

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1Structural Biology Program, Sloan Kettering Institute, New York, USA, ou_persistent22
2Department of Epigenetics, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243644
3Howard Hughes Medical Institute, Sloan Kettering Institute, New York, USA, ou_persistent22

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Abstract: E3 protein ligases enhance transfer of ubiquitin-like (Ubl) proteins from E2 conjugating enzymes to substrates by stabilizing the thioester-charged E2~Ubl in a closed configuration optimally aligned for nucleophilic attack. Here, we report biochemical and structural data that define the N-terminal domain of the Homo sapiens ZNF451 as the catalytic module for SUMO E3 ligase activity. The ZNF451 catalytic module contains tandem SUMO-interaction motifs (SIMs) bridged by a Pro-Leu-Arg-Pro (PLRP) motif. The first SIM and PLRP motif engage thioester-charged E2~SUMO while the next SIM binds a second molecule of SUMO bound to the back side of E2. We show that ZNF451 is SUMO2 specific and that SUMO modification of ZNF451 may contribute to activity by providing a second molecule of SUMO that interacts with E2. Our results are consistent with ZNF451 functioning as a bona fide SUMO E3 ligase.

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Language(s): eng - English

Dates: Date issued: 2015-11-02

Publication Status: Issued

Pages: 8

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Rev. Type: Peer

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Title: Nature Structural & Molecular Biology

Source Genre: Journal

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Pages: 8 Volume / Issue: 22 (12) Sequence Number: - Start / End Page: 968 - 975 Identifier: -