› 1chn

X-ray diffraction
1.76Å resolution

MAGNESIUM BINDING TO THE BACTERIAL CHEMOTAXIS PROTEIN CHEY RESULTS IN LARGE CONFORMATIONAL CHANGES INVOLVING ITS FUNCTIONAL SURFACE

Released:
DOI: 10.2210/pdb1chn/pdb
PDB entry 1chn coloured by chain, front view.
PDB entry 1chn coloured by chain, side view.
PDB entry 1chn coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface.
Bellsolell L, Prieto J, Serrano L, Coll M
J Mol Biol 238 489-95 (1994)
PMID: 8176739

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142405 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chemotaxis protein CheY Chain: A
Molecule details ›
Chain: A
Length: 128 amino acids
Theoretical weight: 13.98 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0AE67 (Residues: 2-129; Coverage: 99%)
Gene names: JW1871, b1882, cheY
Sequence domains: Response regulator receiver domain
Structure domains: Rossmann fold

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 29.9Å b: 44.4Å c: 46.9Å
α: 90° β: 102.9° γ: 90°
R-values:
R R work R free
0.191 0.191 not available
Expression system: Not provided

Quick links

Citations

8 review citations

Two-component signal transduction.
Stock et al. (2000)
7 more

19 mentions without citation

Anchor residues in protein-protein interactions.
Rajamani et al. (2004)
18 more