Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 22, Issue 12, Pages 968-975Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3116
Keywords
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Funding
- Offices of Biological and Environmental Research and of Basic Energy Sciences of the US Department of Energy (DOE)
- National Center for Research Resources [P41RR012408]
- National Institute of General Medical Sciences (NIGMS) of the US National Institutes of Health (NIH) [P41GM103473]
- NIGMS from the NIH [P41 GM103403]
- NIH Office of Research Infrastructure Programs High End Instrumentation grant [S10 RR029205]
- Advanced Photon Source, a DOE Office of Science User Facility operated for the DOE Office of Science by Argonne National Laboratory [DE-AC02-06CH11357]
- NIGMS of the NIH [GM065872]
- NIH-National Cancer Institute Cancer Center Support Grant [P30 CA008748]
- Max Planck Society
- Deutsche Forschungsgemeinschaft [DFG-SPP1365 PI 917/2-1]
- Fonds de Recherche du Quebec-Sante
- Investigator of the Howard Hughes Medical Institute
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E3 protein ligases enhance transfer of ubiquitin-like (UbI) proteins from E2 conjugating enzymes to substrates by stabilizing the thioester-charged E2 similar to UbI 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 similar to 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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