EC Number   |
|---|
   6.2.1.45 | 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 |
| 6.2.1.45 | enzyme exists in two splice variants. To obtain high resolution crystals of UBA5, the N-terminal region of the long isoform, residues 156, are deleted and residues 330404 of the C-terminal domain are also removed. The removal of the CTD thus does not abrogate formation of the UBA5-UFM1 thioester intermediate. Crystals to 2.0 A resolution, and molecular replacement based on PDB structure 1ZFN. Structure shows similarities to both E1 and E1-like enzymes and is composed of an ATP-binding domain that consists of an eight-stranded beta-sheet surrounded by seven alpha-helices. UBA5 maintains a zinc-binding site that is coordinated by four cysteines with tetrahedral geometry |
| 6.2.1.45 | molecular modelling based on the crystal structure of Saccharomyces cerevisiae E1 and Mus musculus E1 and molecular dynamics simulation in water of the human E1-Ub complex |
| 6.2.1.45 | NMR structural studies of the first catalytic cysteine half domain FCCH, interaction studies of FCCH and the other catalytic E1 domain SCCH, second catalytic cysteine half-domain. The E1 has several domains, an adenylation domain, composed of an active and inactive adenylation subdomains, and a catalytic cysteine domain, and smaller accessory domains: a four helix bundle and a ubiquitin fold domain. NMR cannot detect interactions between the FCCH and ubiquitin, or betweenween FCCH and SCCH if they are on separate poypeptide chains |
| 6.2.1.45 | purified recombinant N-terminal enzyme domains comprising residues 1-439, hanging drop vapor diffusion method, mixing of 0.0015 ml of 15 mg/ml protein in 10mM Tris-HCl, pH 8.0, 150mM NaCl, and 2 mM DTT, with 0.0015 ml of reservoir solution containing 0.1 M Na3-citrate, pH 5.6, and 3.2 M NH4Ac, microseeding, 3 days, 21°C, X-ray diffraction structure determination and analysis at 2.75 A resolution |
| 6.2.1.45 | purified UBA5-UFM1 complex, containing both the adenylation domain and the UIS of UBA5, X-ray diffraction structure determination and analysis at 1.85-2.10 A |
| 6.2.1.45 | to 2.0 A resolution using molecular replacement based on PDB entry 1ZFN. UBA5 structure shows similarities to both E1 and E1-like enzymes and is composed of an ATP-binding domain that consists of an eight-stranded beta-sheet surrounded by seven alpha-helices. UBA5 maintains a zinc-binding site that is coordinated by four cysteines with tetrahedral geometry |
