EC Number   |
|---|
   2.3.2.27 | 2.9 A crystal structure of the ubiquitin ligase CHIP U-box domain complexed with UbcH5a. CHIP binds to UbcH5 and Ubc13 through similar specificity determinants located on the long loops and central helix of the CHIP U-box, and on the N-terminal helix and loops L4 and L7 of its cognate E2 enzymes including a key S-P-A motif. The determinants make different relative contributions to the overall interactions between CHIP and the two E2 enzymes. CHIP undergoes auto-ubiquitination by UbcH5 but not by Ubc13-Uev1a. Instead, CHIP drives the formation of unanchored polyubiquitin by Ubc13-Uev1a. CHIP also interacts productively with the class III E2 enzyme Ube2e2 |
| 2.3.2.27 | crystal structure of ZNRF1 C-terminal domain in complex with Ube2N. The domain binds Ube2N exclusively via its RING domain. The ZNRF1:Ube2N interface contains three salt-bridges/H-bonds involving Glu183 of ZNRF1 and Arg14/Lys10 of Ube2N |
| 2.3.2.27 | crystallization of isoform parkin protein residues 141-465 including RING 0 and RING-between-RING domains. The protein is assembled into two compact domain groups separated by linkers. The catalytic network consists of residues C431 and H433. Parkin functions as a RING/HECT hybrid ubiquitin ligase |
| 2.3.2.27 | hanging drop vapor diffusion method, using either 1.0-1.4 M potassium/sodium tartrate /0.1M CHES pH 9.5 /0.2M LiSO4, or 0.5-0.55 M trisodium citrate/0.1 M citric acid pH 5.2/0.2 M lithium acetate, at room temperature |
| 2.3.2.27 | heterodimeric structure of the complex of Ring1b and Bmi1. Complex formation depends on an N-terminal arm of Ring1b that embraces the Bmi1 Ring-domain. Catalytic activity resides in Ring1b and not in Bmi1 |
| 2.3.2.27 | in complex with polycomb group RING finger proteins PCGF5 or PCGF4 and E2 enzyme UbcH5. RING1B binds directly to UbcH5c, with the PCGF partner making no contacts with the E2. The catalytically critical hydrogen bond between RING1B R91 and the backbone carbonyl of UbcH5c Q92 is present in both the structures, consistent with an activated conformation of the E2. Differences between the PCGF4 and PCGF5 ternary complex structures are found at the N termini of the PCGF and RING1B |
| 2.3.2.27 | isoform Rnf4 trimeric complex with UbcH5a and ubiquitin. E2 enzyme UbcH5a is linked by an isopeptide bond to ubiquitin. UbcH5a contacts a single protomer of the RING, and ubiquitin is folded back onto the UbcH5a by contacts from both RING protomers. The C-terminal tail of ubiquitin is locked into an active site groove on UbcH5a by an intricate network of interactions, resulting in changes at the UbcH5a active site |
| 2.3.2.27 | RNF8(345-485)/Ubc13-Ub complex, hanging drop vapor diffusion method, using |
| 2.3.2.27 | solution structure of the isoform HHARI RING2 domain, the key portion of this E3 ligase required for the RING/HECT hybrid mechanism. The domain possesses two Zn2+-binding sites and a single exposed cysteine used for ubiquitin catalysis. A structural comparison of the RING2 domain with the HECT E3 ligase NEDD4 reveals a near mirror image of the cysteine and histidine residues in the catalytic site. A tandem pair of aromatic residues exists near the C-terminus of the HHARI RING2 domain that is conserved in other RING-in-Between-RING E3 ligases |
| 2.3.2.27 | structure of dimeric Ring finger domain of MEX3C and comparison with the complex structure of MDM2/MDMX-UbcH5b-Ub. The Ring finger domain of MEX3C acts as a ubiquitin E3 ligase in vitro, cooperating with E2 enzymes UbcH5b and UbcH5c to mediate ubiquitination |
