› 4kgk

X-ray diffraction
2.95Å resolution

Bacterial tRNA(HIS) Guanylyltransferase (Thg1)-Like Protein in complex with GTP

Released:
DOI: 10.2210/pdb4kgk/pdb
PDB entry 4kgk coloured by chain, front view.
PDB entry 4kgk coloured by chain, side view.
PDB entry 4kgk coloured by chain, top view.
Source organism: Bacillus thuringiensis serovar israelensis ATCC 35646
Primary publication:
Structural studies of a bacterial tRNA(HIS) guanylyltransferase (Thg1)-like protein, with nucleotide in the activation and nucleotidyl transfer sites.
Hyde SJ, Rao BS, Eckenroth BE, Jackman JE, Doublié S
OpenAccess logo PLoS One 8 e67465 (2013)
PMID: 23844012

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-220550 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thg1-like uncharacterized protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 245 amino acids
Theoretical weight: 28.51 KDa
Source organism: Bacillus thuringiensis serovar israelensis ATCC 35646
Expression system: Escherichia coli
Structure domains: Alpha-Beta Plaits

Ligands and Environments

2 bound ligands:
Ligand GTP 8 x GTP
Ligand MG 11 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P41
Unit cell:
a: 111.254Å b: 111.254Å c: 129.124Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.229
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The expanding field of non-canonical RNA capping: new enzymes and mechanisms.
Wiedermannová et al. (2021)
1 more

1 mention without citation

Structural studies of a bacterial tRNA(HIS) guanylyltransferase (Thg1)-like protein, with nucleotide in the activation and nucleotidyl transfer sites.
Hyde et al. (2013)