› 1rfl

Solution NMR

NMR data driven structural model of G-domain of MnmE protein

Released:
DOI: 10.2210/pdb1rfl/pdb
PDB entry 1rfl coloured by chain, ensemble of 20 models, front view.
PDB entry 1rfl coloured by chain, ensemble of 20 models, side view.
PDB entry 1rfl coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
Structural insights into the GTPase domain of Escherichia coli MnmE protein.
Monleón D, Martínez-Vicente M, Esteve V, Yim L, Prado S, Armengod ME, Celda B
Proteins 66 726-39 (2007)
PMID: 17143896

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150492 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA modification GTPase MnmE Chain: A
Molecule details ›
Chain: A
Length: 172 amino acids
Theoretical weight: 18.72 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P25522 (Residues: 210-377; Coverage: 37%)
Gene names: JW3684, b3706, mnmE, thdF, trmE
Sequence domains:
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: NMR restraints were obtained from the backbone assignment (TALOS analysis for dihedral angle constraints) and from the 15N-edited 3D NOESY. Additional structural information was obtained from the homologous GTPAse protein structures.
Expression system: Escherichia coli

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Citations

1 review citation

The universally conserved prokaryotic GTPases.
Verstraeten et al. (2011)
4 other articles

1 mention without citation

Prediction of Protein Structure Using Surface Accessibility Data.
Hartlmüller et al. (2016)