Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

2.7.7.52: RNA uridylyltransferase

This is an abbreviated version!
For detailed information about RNA uridylyltransferase, go to the full flat file.

Word Map on EC 2.7.7.52

Reaction

UTP
+
RNAn
=
diphosphate
+
RNAn+3'-U

Synonyms

3' terminal uridylyl transferase, 3'-terminal uridylyl transferase 1, At2g45620, caffeine-induced death suppressor protein 1, Cid1, GLD2, HESO1, MEAT1, mitochondrial editosome-like complex associated TUTase 1, More, RET, RET1, RET2, RNA editing TUTase, RNA silencing protein 1, Rsp1, Tailor, TbMP57 TUTase, TbTUT3, TbTUT4, terminal RNA uridylyltransferase, terminal U transferase (TUTase), terminal uridylyl transferase, terminal uridylyltransferase, terminal uridylyltransferase Tailor, TNTase CG1091, TUT, TUT1, TUT2, TUT4, TUT7, TUTase, TUTase 1, TUTase 2, TUTase 3, TUTase 4, TUTase4, TUTase6, TUTase7, U6 snRNA-specific terminal uridylyltransferase, U6-TUTase, uridylyltransferase, terminal, URT1, UTP: RNA uridylyltransferase, UTP:RNA uridylyltransferase 1, Zcchc11, ZCCHC6

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.52 RNA uridylyltransferase

Crystallization

Crystallization on EC 2.7.7.52 - RNA uridylyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme D547A, sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.5, 10% (w/v) PEG 6000 and 5% (w/v) 2-methyl-2,4-pentanediol
enzyme bound to uridine-5'-[(alpha,beta)-imido]triphosphate, hanging drop vapor diffusion method, using 20% (v/v) glycerol ethoxylate. Enzyme bound to GpU, sitting drop vapor diffusion method, using 30% (v/v) glycerol ethoxylate and 60 mM sodium malonate, pH 7.0. Enzyme bound to CACAGU, hanging drop vapor diffusion method, using 35% (v/v) glycerol ethoxylate and 75 mM sodium malonate, pH 7.0. Enzyme bound to U6 RNA, sitting drop vapor diffusion method, using 35% (v/v) glycerol ethoxylate and 90 mM sodium malonate, pH 7.0
enzyme residues 202-560 and enzyme in complex with RNA stretches 5 -AGU-3 and 5 -AGUU-3 , sitting drop vapor diffusion method, using 0.1 M Tris-HCl, pH 8.4, 50 mM NaCl, 0.2 M lithium sulfate monohydrate and 15% (w/v) PEG3350
apoenzyme and enzyme in complex with UTP or ATP, hanging drop vapor diffusion method, using 13-15% (w/v) PEG3350 as the precipitant
Lin28-interacting module of TUT4, sitting drop vapor diffusion method, using 100 mM HEPES-NaOH, pH 7.0, 20% (w/v) PEG3350, 3% (v/v) 2-methyl-2,4-pentanediol, 200mM ammonium citrate, and 3% (w/v) 1,5 diaminopentane dihydrochloride
purified recombinant N-terminally His-tagged TUT4, free or with bound 2'-deoxyribonucleoside, at a concentration of 10 mg/mL in 10 mM HEPES, pH 7.6, 70 mM KCl, 0.5 mM DTT, and in presence of 4 mM MgCl2 and 0.05 mM UTP, screening with commercial crystallization screens, vapor diffusion technique, 4°C, cryoprotection by 15% glycerol, X-ray diffraction structure determination and analysis at 2.0-2.4 A resolution
small plate-like co-crystals of purified recombinant N-terminally His-tagged TbTUT4 and UTP grow in 100 mM sodium cacodylate (pH 6.5), 200 mM calcium acetate, 18% (w/v) PEG-8000, crystal structure reveals two significantly different conformations of this TUTase:one molecule is in a relatively open apo confirmation, whereas the other displays a more compact TUTase-UTP complex
structure of apoenzyme and in complex with UTP, to 1.56 A and 1.95 A resolution, respectively. Enzyme possesses a bridging domain, which extends from the C-terminal domain and makes hydrophobic contacts with the N-terminal domain, thereby creating a cavity adjacent to the UTP-binding site. Enzyme shows no appreciable conformational change upon UTP binding and apparently does not require RNA substrate to select a cognate nucleoside triphosphate.
TUT4 in complex with UTP, X-ray diffraction structure analysis
-