› 1vlz

X-ray diffraction
2.05Å resolution

UNCOUPLED PHOSPHORYLATION AND ACTIVATION IN BACTERIAL CHEMOTAXIS: THE 2.1 ANGSTROM STRUCTURE OF A THREONINE TO ISOLEUCINE MUTANT AT POSITION 87 OF CHEY

Released:
DOI: 10.2210/pdb1vlz/pdb
PDB entry 1vlz coloured by chain, front view.
PDB entry 1vlz coloured by chain, side view.
PDB entry 1vlz coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.1-A structure of a threonine to isoleucine mutant at position 87 of CheY.
Ganguli S, Wang H, Matsumura P, Volz K
J Biol Chem 270 17386-93 (1995)
PMID: 7615544

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142407 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chemotaxis protein CheY Chains: A, B
Molecule details ›
Chains: A, B
Length: 128 amino acids
Theoretical weight: 13.99 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 54.04Å b: 72.47Å c: 36.15Å
α: 90° β: 109.06° γ: 90°
R-values:
R R work R free
0.156 not available not available
Expression system: Not provided

Quick links

Citations

3 review citations

The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes.
Falke et al. (1997)
2 more

1 mention without citation

Statistical analysis of interface similarity in crystals of homologous proteins.
Xu et al. (2008)