6.2.1.45: E1 ubiquitin-activating enzyme

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For detailed information about E1 ubiquitin-activating enzyme, go to the full flat file.

Reaction

Synonyms

AtUBA1, AtUBA2, E1, E1 ubiquitin-activating enzyme, HsUba1a, non-canonical ubiquitin activating enzyme, SUMO E1, UB activating enzyme, Ub E1 activating enzyme, Ub-activating enzyme, Ub-activating ligase, Uba1, Uba1/E1, Uba1a, UBA1p, UBA2, UBA5, Uba6, UBA7, UBE1, UBE1DC1, UBE1DC1A, UBE1DC1B, UBE1L, UBE1L2, ubiquitin activating enzyme, ubiquitin activating enzyme 2, ubiquitin activating enzyme E1, ubiquitin activating enzyme E1-like, ubiquitin E1, ubiquitin protein ligase E1, Ubiquitin-activating enzyme, ubiquitin-activating enzyme (E1), ubiquitin-activating enzyme 1, ubiquitin-activating enzyme 5, ubiquitin-activating enzyme 6, ubiquitin-activating enzyme E1, ubiquitin-activating enzyme E1 domain-containing protein 1, ubiquitin-activating enzyme E1-domain containing 1, ubiquitin-activating enzyme, UBE1, ubiquitin-conjugating enzyme, ubiquitin-like modifier-activating enzyme 1, ubiquitin-like modifier-activating enzyme 5, ubiquitin-like modifier-activating enzyme 6, ubiquitin-like modifier-activating enzyme 7 isoform X2

ECTree

     6 Ligases

         6.2 Forming carbon-sulfur bonds

             6.2.1 Acid-thiol ligases

                6.2.1.45 E1 ubiquitin-activating enzyme

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Results	in table
4	Activating Compound
2393	AA Sequence
7	Application
31	Cloned(Commentary)
16	Cofactor
7	Crystallization (Commentary)
861	Disease/ Diagnostics
4	Expression
43	General Information
3	IC50 Value
27	Inhibitors
1	Ki Value [mM]
28	KM Value [mM]
11	Localization
17	Metals/Ions
16	Molecular Weight [Da]
25	Natural Substrates/ Products (Substrates)
52	Organism
1	Pathway
42	PDB ID
7	pH Optimum
1	pI Value
3	Posttranslational Modification
33	Protein Variants
16	Purification (Commentary)
5	Reaction
49	Reference
62	Source Tissue
2	Storage Stability
55	Substrates and Products (Substrate)
16	Subunits
100	Synonyms
1	Systematic Name
7	Temperature Optimum [°C]
30	Turnover Number [1/s]

Crystallization

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Crystallization on EC 6.2.1.45 - E1 ubiquitin-activating enzyme

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

enzyme exists in two splice variants. To obtain high resolution crystals of UBA5, the N-terminal region of the long isoform, residues 1–56, are deleted and residues 330–404 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

Homo sapiens

Q9GZZ9

709113

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

Homo sapiens

P22314

709769

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

Homo sapiens

P22314

733532

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

Homo sapiens

Q9GZZ9

744655

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

Homo sapiens

Q9GZZ9

709113

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

Mus musculus

Q02053

725840

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

Saccharomyces cerevisiae

P52488

728546