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2.3.2.23: E2 ubiquitin-conjugating enzyme

This is an abbreviated version!
For detailed information about E2 ubiquitin-conjugating enzyme, go to the full flat file.

Word Map on EC 2.3.2.23

Reaction

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
+
[E2 ubiquitin-conjugating enzyme]-L-cysteine
=
[E1 ubiquitin-activating enzyme]-L-cysteine
+
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine

Synonyms

alpha spectrin, ARIH1, At1g78870, At2g02760, CDC34, Cdc34B, Ci0100152677, E2 enzyme, E2 Ub-conjugating enzyme, E2 ubiquitin conjugating enzyme, E2 ubiquitin-conjugating enzyme, E2-20K, E2-25K, E2-conjugating enzyme, E2-ubiquitin conjugating enzyme, FANCT, HOYS7, Mms2, NCUBE1, NEDD8-activating enzyme E1 catalytic subunit, Pex4, Rad6a, RAD6B, Rad6p, SCEI, SUMO E2 conjugating enzyme, SUMO E2 enzyme, SUMO-1-conjugating enzyme Ubc9, SUMO-conjugating enzyme UBC9, UBA2, Uba3, UBA6-specific E2 enzyme 1, UBC E2, Ubc-18, Ubc1, Ubc11, Ubc13, Ubc2, Ubc35, Ubc3B, Ubc4, Ubc4/5, Ubc5a, Ubc6, UBC6e, UBC7, Ubc8, Ubc9, UbcA1, UBCE4, UbcH10, UBCH2, UbcH3, UbcH5A, UbcH5B, UbcH5C, UbcH5D, UbcH6, UbcH7, UbcH8, UbcH9, UbcM2, UbcM4, Ube2, UBE2A, UBE2B, UBE2C, UBE2D, UBE2D1, ube2d1b, UBE2D2, UBE2D3, UBE2D4, UBE2E1, UBE2E2, UBE2E3, Ube2G, UBE2G1, UBE2G2, UBE2H, Ube2I, Ube2J1, UBE2J2, UBE2K, UBE2L3, UBE2L6, UBE2N, Ube2NL, UBE2Q1, UBE2Q2, UBE2QL, UBE2QL1, Ube2r, UBE2R1, UBE2R2, UBE2S, UBE2T, UBE2U, Ube2V, UBE2V1, UBE2V2, UBE2W, UBE2Z, ubiquitin-conjugating enzyme, ubiquitin-conjugating enzyme (E2), ubiquitin-conjugating enzyme E2, ubiquitin-conjugating enzyme E2 B, ubiquitin-conjugating enzyme E2 D1, ubiquitin-conjugating enzyme E2 G1, ubiquitin-conjugating enzyme E2 Z, ubiquitin-conjugating enzyme E2-20 kDa, ubiquitin-conjugating enzyme E2T, ubiquitination enzyme, Uev1, Uev1A, Uev2, USE1, VvUBC

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.23 E2 ubiquitin-conjugating enzyme

Crystallization

Crystallization on EC 2.3.2.23 - E2 ubiquitin-conjugating enzyme

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
using 20% (w/v) PEG 3350, 0.2 M sodium acetate, and 0.1 M Bis-Tris, pH 6.5
-
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
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)
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
Ube2T in complex with inhibitor 1-(1,3-benzothiazol-2-yl)methanamine, X-ray diffraction crystal structure analysis, PDB ID 5NGZ
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
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
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