EC Number   |
Reference |
|---|
   2.3.2.23 | 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 |
691518 |
| 2.3.2.23 | Cdc34 alone and in complex with E1, and a Cdc34-Ub thioester mimetic representing the product of Uba1-Cdc34 Ub transthiolation, sitting drop method, mixing of 200 nl of 8.7 mg/ml Uba1-Cdc34DELTAdist crosslink and 0.116 mM Ub, 1 mM ATP, and 5 mM MgCl2, with 200 nl of mother liquor containing 0.2 M ammonium sulfate, 25% PEG 3,350, 0.1 M Bis-Tris, pH 6.5, 18°C, for the free Cdc34DELTAdist, hanging drop method is used with 10 mg/ml protein and mother liquor containing 0.06 M zinc acetate, 0.108 M sodium cacodylate, 14.4% PEG 8000, and 20% glycerol, 18°C, a 1.3fold excess of Cdc34 inhibitor CC0651 is used as a crystallization aid, X-ray diffraction structure determination and analysis at 1.65-2.07 A resolution, molecular replacement using structure PDB ID 3CMM as the search model, modeling |
759820 |
| 2.3.2.23 | crystal structure of an E2-Ub oxyester conjugate (Ube2D2) in a closed state showing the interface formed between the E2 crossover helix and the I44 surface of Ub upon binding a RING E3 (BIRC7, PDB ID 4AUQ) |
759030 |
| 2.3.2.23 | crystal structures of the C-terminal ubiquitin fold domain from yeast Uba2 alone and in complex with E2 enzyme Ubc9. Uba2 undergoes remarkable conformational changes during the reaction. The structure of the Uba2 domain-Ubc9 complex reveals interactions unique to Sumo E1 and E2. Comparison with a previous Ubc9-E3 complex structure demonstrates overlap between Uba2 and E3 binding sites on Ubc9, indicating that loading with Sumo and E3-catalyzed transfer to substrates are strictly separate steps |
728546 |
| 2.3.2.23 | mutant C105S/C146S in complex with the soluble domain of peroxisomal membrane protein Pex22. Structure shows a narrowing of the active site cleft, caused by loss of the disulfide bond |
735257 |
| 2.3.2.23 | purified recombinant detagged UBE2Z, microcrystals are grown by mixing of 12 mg/ml protein solution with crystallization solution containing 25% w/v PEG 6000 and 0.1 M Tris, pH 8.0, a seed stock is generated from these microcrystals and used in cross-seeding, diffraction quality crystals grow at room temperature in 8-25% w/v PEG 1500, 0.1 M D-malic acid-MES-TRIS buffer at pH 5.0-7.5, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using the structure of UBE2D3 (PDB ID 1X23) as the search model for UBE2Z. The determined structure lacks the N-terminal 98 residues of the protein corresponding to the UBE2Z N-terminal extension |
759478 |
| 2.3.2.23 | recombinant enzyme, N-terminally His-tagged, subcloned in Escherichia coli BL21(DE2), via pET28 vector, purified using Ni-NTA column and HiLoad 16/60 Superdex 75 gel filtration column, diffracted X-rays to 1.7 A. The crystal belongs to space group C2 |
723874 |
| 2.3.2.23 | Ube2T in complex with inhibitor 1-(1,3-benzothiazol-2-yl)methanamine, X-ray diffraction crystal structure analysis, PDB ID 5NGZ |
759600 |
| 2.3.2.23 | using 20% (w/v) PEG 3350, 0.2 M sodium acetate, and 0.1 M Bis-Tris, pH 6.5 |
737253 |
