› 5m7o

X-ray diffraction
2.2Å resolution

Crystal structure of NtrX from Brucella abortus processed with the CrystalDirect automated mounting and cryo-cooling technology

Released:
DOI: 10.2210/pdb5m7o/pdb
PDB 5m7o coloured by chain and viewed from the front.
PDB 5m7o coloured by chain and viewed from the side.
PDB 5m7o coloured by chain and viewed from the top.
Source organism: Brucella abortus str. 2308 A
Primary publication:
Three-dimensional structure of full-length NtrX, an unusual member of the NtrC family of response regulators.
Fernández I, Cornaciu I, Del Carmen Carrica M, Uchikawa E, Hoffmann G, Sieira R, Márquez JA, Goldbaum FA
J. Mol. Biol. (2017)
PMID: 28088479

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nitrogen assimilation regulatory protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 454 amino acids
Theoretical weight: 50.28 KDa
Source organism: Brucella abortus str. 2308 A
Expression system: Escherichia coli
UniProt:
  • Canonical: C4IRH0 (Residues: 1-453; Coverage: 100%)
Gene name: BAAA_2000042
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2221
Unit cell:
a: 124.778Å b: 191.228Å c: 111.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.227 0.269
Expression system: Escherichia coli

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Citations

1 review citation

Role of the Extremolytes Ectoine and Hydroxyectoine as Stress Protectants and Nutrients: Genetics, Phylogenomics, Biochemistry, and Structural Analysis.
Czech et al. (2018)
4 other articles