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2.1.1.260: rRNA small subunit pseudouridine methyltransferase Nep1

This is an abbreviated version!
For detailed information about rRNA small subunit pseudouridine methyltransferase Nep1, go to the full flat file.

Word Map on EC 2.1.1.260

Reaction

S-adenosyl-L-methionine
+
pseudouridine1191 in yeast 18S rRNA
=
S-adenosyl-L-homocysteine
+
N1-methylpseudouridine1191 in yeast 18S rRNA

Synonyms

Bowen-Conradi syndrome protein, Emg1, Emg1p, essential for mitotic growth 1, N1-specific pseudouridine methyltransferase, Nep1, Nep1 methyltransferase, Nep1p, nucleolar essential protein 1, pseudouridine N1-methyltransferase, pseudouridine-N1-specific methyltransferase

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.260 rRNA small subunit pseudouridine methyltransferase Nep1

Crystallization

Crystallization on EC 2.1.1.260 - rRNA small subunit pseudouridine methyltransferase Nep1

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant detagged wild-type and selenomethionine-labeled afNep1 dimer bound to S-adenosyl homocysteine, X-ray diffraction structure determination and analysis at 1.45-2.0 A resolution
Nep1 in its free form and bound to S-adenosylhomocysteine or the antibiotic and general methyltransferase inhibitor sinefungin, hanging drop vapour diffusion method, 10-15 mg/ml protein in 100 mM BisTris-propane buffer, pH 9.5, 6-10% PEG 400, 30-48% glycerol, and 0-400 mM trimethylamine-N-oxide, at 4°C, crystals of the selenomethionine containing protein in the presence or absence of a 3fold excess of S-adenosyl-L-homocysteine are grown under similar conditions at 16°C, X-ray diffraction structure determination and analysis at 2.2 A, 2.15 A, and 2.25 A resolution, respectively
recombinant detagged scNep1 dimer bound to S-adenosyl homocysteine and in complexes with RNA, i.e. one molecule and two molecules of cognate RNA, X-ray diffraction structure determination and analysis at 1.80-1.90 A and at 3.00 A resolution, respectively
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