› 2idm

X-ray diffraction
2Å resolution

2.00 A Structure of T87I/Y106W Phosphono-CheY

Released:
DOI: 10.2210/pdb2idm/pdb
PDB entry 2idm coloured by chain, front view.
PDB entry 2idm coloured by chain, side view.
PDB entry 2idm coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptides.
McAdams K, Casper ES, Matthew Haas R, Santarsiero BD, Eggler AL, Mesecar A, Halkides CJ
Arch Biochem Biophys 479 105-13 (2008)
PMID: 18801331

Function and Biology Details

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

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: 14.1 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
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 ACT 1 x ACT
1 modified residue:
Ligand CYQ 1 x CYQ

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P212121
Unit cell:
a: 40.091Å b: 50.544Å c: 52.956Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.233 0.328
Expression system: Escherichia coli

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Citations

1 review citation

Survey of the year 2008: applications of isothermal titration calorimetry.
Falconer et al. (2010)
3 other articles

2 mentions without citation

Structural Conservation and Adaptation of the Bacterial Flagella Motor.
Carroll et al. (2020)
1 more