2mdp

The bacteriophage T7 encoded inhibitor (gp1.2) of E. coli dGTP triphosphohydrolaseThe bacteriophage T7 encoded inhibitor (gp1.2) of E. coli dGTP triphosphohydrolase

Structural highlights

2mdp is a 1 chain structure with sequence from Escherichia phage T7. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GP12_BPT7 Plays a role in increasing the intracellular pool of dGTP. Interacts with and inhibits host dGTPase/dgt. The complex made of the host dGTPase and gene 1.2 protein creates a GTP-binding site of high affinity. Subsequent binding of GTP to the enzyme-inhibitor complex inhibits its dissociation.^[1] ^[2]

References

↑ Nakai H, Richardson CC. The gene 1.2 protein of bacteriophage T7 interacts with the Escherichia coli dGTP triphosphohydrolase to form a GTP-binding protein. J Biol Chem. 1990 Mar 15;265(8):4411-9. PMID:2155228
↑ Myers JA, Beauchamp BB, Richardson CC. Gene 1.2 protein of bacteriophage T7. Effect on deoxyribonucleotide pools. J Biol Chem. 1987 Apr 15;262(11):5288-92. PMID:3549718

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OCA

[1] Nakai H, Richardson CC. The gene 1.2 protein of bacteriophage T7 interacts with the Escherichia coli dGTP triphosphohydrolase to form a GTP-binding protein. J Biol Chem. 1990 Mar 15;265(8):4411-9. PMID:2155228

[2] Myers JA, Beauchamp BB, Richardson CC. Gene 1.2 protein of bacteriophage T7. Effect on deoxyribonucleotide pools. J Biol Chem. 1987 Apr 15;262(11):5288-92. PMID:3549718

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