Structural mechanisms of autoinhibition and substrate recognition by the ubiquitin ligase HACE1

Düring J, Wolter M, Toplak J, Torres C, Dybkov O, Fokkens T, Bohnsack K, Urlaub H, Steinchen W, Dienemann C, Lorenz S
Nature Structural & Molecular Biology (2024 Feb 08)

doi: 10.1038/s41594-023-01203-4 		Submitted to SASBDB: 2023 Dec 5
Published in SASBDB:

SASDTC5 – Full-length E3 ubiquitin-protein ligase HACE1

E3 ubiquitin-protein ligase HACE1 experimental SAS data
GASBOR model
Sample: E3 ubiquitin-protein ligase HACE1 dimer, 205 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 50 mM NaCl, 5 mM DTT, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Apr 21
RgGuinier 5.2 nm
Dmax 16.4 nm
VolumePorod 379 nm3

SASDTD5 – N-terminally truncated E3 ubiquitin-protein ligase HACE1

E3 ubiquitin-protein ligase HACE1 experimental SAS data
MULTIFOXS model
Sample: E3 ubiquitin-protein ligase HACE1 monomer, 100 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 50 mM NaCl, 5 mM DTT, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Apr 21
RgGuinier 4.6 nm
Dmax 17.8 nm
VolumePorod 219 nm3