› 7tu8

Electron Microscopy
2.6Å resolution

Structure of the L. blandensis dGTPase H125A mutant bound to dGTP and dATP

Released:
DOI: 10.2210/pdb7tu8/pdb
PDB entry 7tu8 coloured by chain, front view.
PDB entry 7tu8 coloured by chain, side view.
PDB entry 7tu8 coloured by chain, top view.
Source organism: Leeuwenhoekiella blandensis MED217
Primary publication:
High-resolution structures of the SAMHD1 dGTPase homolog from Leeuwenhoekiella blandensis reveal a novel mechanism of allosteric activation by dATP.
Klemm BP, Sikkema AP, Hsu AL, Horng JC, Hall TMT, Borgnia MJ, Schaaper RM
J Biol Chem 298 102073 (2022)
PMID: 35643313
Related structures: EMD-26129

Function and Biology Details

Reaction catalysed: 
dGTP + H(2)O = deoxyguanosine + triphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107253 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
HD domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 464 amino acids
Theoretical weight: 52.66 KDa
Source organism: Leeuwenhoekiella blandensis MED217
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A3XHN1 (Residues: 3-442; Coverage: 99%)
Gene name: MED217_16760
Sequence domains: HD domain

Ligands and Environments

3 bound ligands:
Ligand DGT 6 x DGT
Ligand DTP 6 x DTP
Ligand MG 12 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.6Å
Relevant EMDB volumes: EMD-26129
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Mechanism by which T7 bacteriophage protein Gp1.2 inhibits Escherichia coli dGTPase.
Klemm et al. (2022)
1 more

1 mention without citation

High-resolution structures of the SAMHD1 dGTPase homolog from Leeuwenhoekiella blandensis reveal a novel mechanism of allosteric activation by dATP.
Klemm et al. (2022)