Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.7 Nucleotidyltransferases
ID:2.7.7.88
Description:GDP polyribonucleotidyltransferase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.7.88
BRENDA Enzyme Link: BRENDA 2.7.7.88
KEGG Enzyme Link: KEGG2.7.7.88
BioCyc Enzyme Link: BioCyc 2.7.7.88
ExPASy Enzyme Link: ExPASy2.7.7.88
EC2PDB Enzyme Link: EC2PDB 2.7.7.88
ExplorEnz Enzyme Link: ExplorEnz 2.7.7.88
PRIAM enzyme-specific profiles Link: PRIAM 2.7.7.88
IntEnz Enzyme Link: IntEnz 2.7.7.88
MEDLINE Enzyme Link: MEDLINE 2.7.7.88
MSA:

2.7.7.88;

Phylogenetic Tree:

2.7.7.88;

Uniprot:
M-CSA:
RHEA:46292 a 5'-triphospho-(purine-ribonucleotide)-[mRNA] + GDP + H(+) = a 5'-(5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] + diphosphate
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[P;H0;+0:4](=[*:5])(-[*:6])-[O;H0;+0:7]-[*:8].[H+;H0:9]>>[*:1]-[O;H0;+0:2]-[P;H0;+0:4](-[*:3])(=[*:5])-[*:6].[*:8]-[OH;+0:7]
Reaction
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References

TitleAuthorsDatePubMed ID
Signature motifs of GDP polyribonucleotidyltransferase, a non-segmented negative strand RNA viral mRNA capping enzyme, domain in the L protein are required for covalent enzyme-pRNA intermediate formation.Neubauer J, Ogino M, Green TJ, Ogino T2016 Jan 826602696
An unconventional pathway of mRNA cap formation by vesiculoviruses.Ogino T, Banerjee AK2011 Dec21945214
Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase.Ogino T, Yadav SP, Banerjee AK2010 Feb 2320142503
The HR motif in the RNA-dependent RNA polymerase L protein of Chandipura virus is required for unconventional mRNA-capping activity.Ogino T, Banerjee AK2010 May20107017
Formation of guanosine(5')tetraphospho(5')adenosine cap structure by an unconventional mRNA capping enzyme of vesicular stomatitis virus.Ogino T, Banerjee AK2008 Aug18495767
Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus.Ogino T, Banerjee AK2007 Jan 1217218273