› 2ld6

Solution NMR

Solution Structure of Histidine Phosphotransfer Domain of CheA

Released:
DOI: 10.2210/pdb2ld6/pdb
PDB entry 2ld6 coloured by chain, ensemble of 26 models, front view.
PDB entry 2ld6 coloured by chain, ensemble of 26 models, side view.
PDB entry 2ld6 coloured by chain, ensemble of 26 models, top view.
Source organism: Thermotoga maritima
Primary publication:
The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima.
Vu A, Hamel DJ, Zhou H, Dahlquist FW
OpenAccess logo J Biomol NMR 51 49-55 (2011)
PMID: 21947914

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 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: 139 amino acids
Theoretical weight: 15.78 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q56310 (Residues: 1-131; Coverage: 20%)
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
Chemical shift assignment: 81%
Refinement method: DGSA-distance geometry simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.
Minato et al. (2017)

3 mentions without citation

Conformational Transitions that Enable Histidine Kinase Autophosphorylation and Receptor Array Integration.
Greenswag et al. (2015)
2 more