› 1sut

Solution NMR

NMR STUDY OF THE PROLINE REPEAT FROM TUS

Released:
DOI: 10.2210/pdb1sut/pdb
PDB entry 1sut coloured by chain, ensemble of 10 models, front view.
PDB entry 1sut coloured by chain, ensemble of 10 models, side view.
PDB entry 1sut coloured by chain, ensemble of 10 models, top view.
Source organism: Escherichia coli K-12
Primary publication:
Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
Butcher DJ, Nedved ML, Neiss TG, Moe GR
Biochemistry 35 698-703 (1996)
PMID: 8547250

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-147754 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA replication terminus site-binding protein Chain: A
Molecule details ›
Chain: A
Length: 22 amino acids
Theoretical weight: 2.61 KDa
Source organism: Escherichia coli K-12
Expression system: Not provided
UniProt:
  • Canonical: P16525 (Residues: 223-244; Coverage: 7%)
Gene names: JW1602, b1610, tau, tus

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

1 review citation

The hunchback and its neighbours: proline as an environmental modulator.
Reiersen et al. (2001)
2 other articles