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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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Datensatz-Permalink: https://hdl.handle.net/someHandle/test/escidoc:902497 Versions-Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-99D0-7
Genre: Zeitschriftenartikel

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 Urheber:
Cappadocia, Laurant1, Autor
Pichler, A.2, Autor           
Lima, Christopher D.1, 3, Autor
Affiliations:
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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 Zusammenfassung: 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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Sprache(n): eng - English
 Datum: 2015-11-02
 Publikationsstatus: Erschienen
 Seiten: 8
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
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 Art des Abschluß: -

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Titel: Nature Structural & Molecular Biology
Genre der Quelle: Zeitschrift
 Urheber:
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Ort, Verlag, Ausgabe: -
Seiten: 8 Band / Heft: 22 (12) Artikelnummer: - Start- / Endseite: 968 - 975 Identifikator: -