› 1tqg

X-ray diffraction
0.98Å resolution

CheA phosphotransferase domain from Thermotoga maritima

Released:
DOI: 10.2210/pdb1tqg/pdb
PDB entry 1tqg coloured by chain, front view.
PDB entry 1tqg coloured by chain, side view.
PDB entry 1tqg coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Helical shifts generate two distinct conformers in the atomic resolution structure of the CheA phosphotransferase domain from Thermotoga maritima.
Quezada CM, Gradinaru C, Simon MI, Bilwes AM, Crane BR
J Mol Biol 341 1283-94 (2004)
PMID: 15321722

Function and Biology Details

Reaction catalysed: 
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176348 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chemotaxis protein CheA Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 11.87 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q56310 (Residues: 4-104; Coverage: 15%)
Gene names: TM_0702, cheA
Sequence domains: Hpt domain
Structure domains: HPT domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P2221
Unit cell:
a: 27.381Å b: 37.419Å c: 87.542Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.211
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
2 more

15 mentions without citation

Regulation of the chemotaxis histidine kinase CheA: A structural perspective.
Muok et al. (2020)
14 more