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

Cappadocia, Laurent; Pichler, Andrea; Lima, Christopher D.

doi:10.1038/nsmb.3116

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

Journal Article · Mon Nov 02 00:00:00 EST 2015 · Nature Structural & Molecular Biology

DOI:https://doi.org/10.1038/nsmb.3116· OSTI ID:1229890

Cappadocia, Laurent ^[1]; Pichler, Andrea ^[2]; Lima, Christopher D. ^[3]

Sloan Kettering Inst., New York, NY (United States). Structural Biology Program
Max Planck Inst. of Immunobiology and Epigenetics, Freiburg (Germany). Dept. of Epigenetics
Sloan Kettering Inst., New York, NY (United States). Structural Biology Program. Howard Hughes Medical Inst.

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. In this paper, 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. Finally, our results are consistent with ZNF451 functioning as a bona fide SUMO E3 ligase.

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Research Organization:: Sloan Kettering Inst., New York, NY (United States); Max Planck Inst. of Immunobiology and Epigenetics, Freiburg (Germany)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Biological and Environmental Research (BER); National Inst. of Health (NIH) (United States); Max Planck Society (Germany); German Research Foundation (DFG)

Grant/Contract Number:: AC02-06CH11357; P41RR012408; P41GM103473; P41 GM103403; S10 RR029205; GM065872; P30 CA008748; DFG-SPP1365 PI 917/2-1

OSTI ID:: 1229890

Journal Information:: Nature Structural & Molecular Biology, Vol. 22, Issue 12; ISSN 1545-9993

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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