› 1jem

Solution NMR

NMR STRUCTURE OF HISTIDINE PHOSPHORYLATED FORM OF THE PHOSPHOCARRIER HISTIDINE CONTAINING PROTEIN FROM BACILLUS SUBTILIS, NMR, 25 STRUCTURES

Released:
DOI: 10.2210/pdb1jem/pdb
PDB entry 1jem coloured by chain, ensemble of 25 models, front view.
PDB entry 1jem coloured by chain, ensemble of 25 models, side view.
PDB entry 1jem coloured by chain, ensemble of 25 models, top view.
Source organism: Bacillus subtilis
Primary publication:
Phosphorylation on histidine is accompanied by localized structural changes in the phosphocarrier protein, HPr from Bacillus subtilis.
Jones BE, Rajagopal P, Klevit RE
Protein Sci 6 2107-19 (1997)
PMID: 9336834

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-140403 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphocarrier protein HPr Chain: A
Molecule details ›
Chain: A
Length: 87 amino acids
Theoretical weight: 9.12 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P08877 (Residues: 2-88; Coverage: 99%)
Gene names: BSU13900, ptsH
Sequence domains: PTS HPr component phosphorylation site
Structure domains: HPr-like

Ligands and Environments

No bound ligands
1 modified residue:
Ligand HIP 1 x HIP

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

Quick links

Citations

2 review citations

High energy exchange: proteins that make or break phosphoramidate bonds.
Robinson et al. (1999)
1 more

1 mention without citation

The many ways that nature has exploited the unusual structural and chemical properties of phosphohistidine for use in proteins.
Kalagiri et al. (2021)