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2.7.7.50: mRNA guanylyltransferase

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

Word Map on EC 2.7.7.50

Reaction

GTP
+
(5')ppPur-mRNA
=
diphosphate
 +
G(5')pppPur-mRNA

Synonyms

A103R, A103R protein, cap guanylyltransferase-methyltransferase, capping enzyme, capping enzyme guanylyltransferase, Ceg1, CET1, CmCeg1, D1 protein, GDP polyribonucleotidyltransferase, GlCeg1, GTase, GTP-RNA guanylyltransferase, GTP:RNA GTase, guanylyltransferase, guanylyltransferase mRNA capping, HCE, L protein, Mce1, messenger RNA guanylyltransferase, More, mRNA capping enzyme, mRNA guanylyl transferase, mRNA-cap, mRNA-capping enzyme, NAD-decapping enzyme, nsP1, NudC, PRNTase, protein lambda2, RNA capping enzyme, RNA guanylyltransferase, RNGTT, TbCgm1, TTM-type RTPase-GTase, VACWR106, VP3

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.50 mRNA guanylyltransferase

Crystallization

Crystallization on EC 2.7.7.50 - mRNA guanylyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytically active native MimiCE-(1-237) protein by vapor diffusion against a precipitant solution containing PEG4000 plus citrate and acetate buffers, X-ray diffraction structure determination and analysis at 1.65-2.9 A resolution
enzyme in complex with either NAD or NMN, hanging drop vapor diffusion method, using either 0.2 M sodium nitrate, 20% PEG-3350 or 1 M LiCl2, 0.1 M HEPES, pH 7.0, and 10% PEG-6000
-
structure of residues 229-567, comprising the minimum enzymatically active human guanylyltransferase domain, to 3.0 A
crystals of RNA guanylyltransferase, i.e. capping enzyme, complexed with a mRNA cap analogue G(5')ppp(5')G, enzyme solution: 15 mg/ml, 1.3 mM GpppG, 50 mM Tris, pH 7.5, 0.4 M NaCl, 2 mM EDTA, 4 mM DTT, mixed with equal volume of equilibration solution: potassium phosphate 50 mM, pH 6.5, 5-10% PEG 8000, 2 mM ZnCl2, 24 h, X-ray structure determination and analysis
-
empirical and thermodynamic integration pKa estimates, along with conventional molecular dynamics simulations based on PDB entries 1ckm and 1ckn. Magnesium binding likely activates the lysine nucleophile by increasing its acidity and by biasing the deprotonated nucleophile into conformations conducive to intermediate formation
GTase in complex with C-terminal domain repeats of RNA polymerase Pol2 reveals a unique docking site on the nucleotidyl transferase domain for an 8-amino-acid Pol2 C-terminal domain segment, S5PPSYSPTS5P, bracketed by two Ser5-PO4 marks. At least one of the two Ser5-PO4-binding sites is required for cell viability and each site is important for cell growth at 37°C. GTase binds the Spt5 C-terminal domain at a separate docking site in the OB-fold domain that captures the Trp4 residue of the Spt5 nonapeptide repeat T1PAW4NSGSK
structures of the complete heterodimer formed by polypeptides D1 and D12. The D1 subunit comprises an N-terminal RNA triphosphatase (TPase)-guanylyltransferase (GTase) module and a C-terminal guanine-N7-methyltransferase (MTase) module. The D12 subunit binds and allosterically stimulates the MTase module. An extensive TPase-GTase interface clamps the GTase nucleotidyltransferase and oligosaccharide-binding fold domains in a closed conformation around GTP