DGTPase

 

Deoxyguanosinetriphosphate triphosphohydrolase (dGTPase) is a triphosphohydrolase that has a preference for dGTP over other dNTPs, they hydrolase dGTP to form deoxyguanosine and triphosphate. Escherichia coli dGTPase (Dgt) has been shown to have a strong single-stranded DNA-binding (ssDNA) activity [PMID:25694425] which is thought to act as an allosteric regulator.

 

Reference Protein and Structure

Sequence
P15723 UniProt (3.1.5.1) IPR020779 (Sequence Homologues) (PDB Homologues)
Biological species
Escherichia coli K-12 (Bacteria) Uniprot
PDB
4x9e - DEOXYGUANOSINETRIPHOSPHATE TRIPHOSPHOHYDROLASE from Escherichia coli with two DNA effector molecules (3.1 Å) PDBe PDBsum 4x9e
Catalytic CATH Domains
1.10.3210.10 CATHdb (see all for 4x9e)
Cofactors
Magnesium(2+) (1)
Click To Show Structure

Enzyme Reaction (EC:3.1.5.1)

dGTP(4-)
CHEBI:61429ChEBI
+
water
CHEBI:15377ChEBI
2'-deoxyguanosine
CHEBI:17172ChEBI
+
triphosphate(5-)
CHEBI:18036ChEBI
+
hydron
CHEBI:15378ChEBI
Alternative enzyme names: Deoxy-GTPase, Deoxyguanosine 5-triphosphate triphosphohydrolase, Deoxyguanosine triphosphatase, Deoxyguanosine triphosphate triphosphohydrolase, Deoxyguanosinetriphosphate triphosphohydrolase,

Enzyme Mechanism

Introduction

The mechanism for this protein has not yet been elucidated.

Catalytic Residues Roles

UniProt PDB* (4x9e)
His69, Asp268, Asp118, His117 His69A, Asp268A, Asp118A, His117A Forms part of the magnesium binding site. metal ligand
Arg442 Arg442B The exact role of this residue is unknown at this time. It is interesting because after DNA binding, it moved closer to the dGTP substrate, which is likely to affect the positioning of the substrate. unknown
*PDB label guide - RESx(y)B(C) - RES: Residue Name; x: Residue ID in PDB file; y: Residue ID in PDB sequence if different from PDB file; B: PDB Chain; C: Biological Assembly Chain if different from PDB. If label is "Not Found" it means this residue is not found in the reference PDB.

Chemical Components

References

  1. Singh D et al. (2015), J Biol Chem, 290, 10418-10429. Structure of Escherichia coli dGTP triphosphohydrolase: a hexameric enzyme with DNA effector molecules. DOI:10.1074/jbc.M115.636936. PMID:25694425.
  2. Seto D et al. (1988), J Biol Chem, 263, 1494-1499. The purification and properties of deoxyguanosine triphosphate triphosphohydrolase from Escherichia coli. PMID:2826481.

Catalytic Residues Roles

Residue Roles
His69A metal ligand
His117A metal ligand
Asp118A metal ligand
Asp268A metal ligand
Arg442B unknown

Chemical Components

Contributors

Gemma L. Holliday