› 1lr1

Solution NMR

Solution Structure of the Oligomerization Domain of the Bacterial Chromatin-Structuring Protein H-NS

Released:
DOI: 10.2210/pdb1lr1/pdb
PDB entry 1lr1 coloured by chain, ensemble of 20 models, front view.
PDB entry 1lr1 coloured by chain, ensemble of 20 models, side view.
PDB entry 1lr1 coloured by chain, ensemble of 20 models, top view.
Source organism: Escherichia coli
Primary publication:
H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein.
Esposito D, Petrovic A, Harris R, Ono S, Eccleston JF, Mbabaali A, Haq I, Higgins CF, Hinton JC, Driscoll PC, Ladbury JE
J Mol Biol 324 841-50 (2002)
PMID: 12460581

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142275 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA-binding protein H-NS Chains: A, B
Molecule details ›
Chains: A, B
Length: 61 amino acids
Theoretical weight: 7.02 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ACF8 (Residues: 2-58; Coverage: 42%)
Gene names: JW1225, b1237, bglY, cur, drdX, h-ns, hns, hnsA, msyA, osmZ, pilG, topS
Sequence domains: H-NS histone-like proteins, N-terminal domain
Structure domains: H-NS histone-like proteins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: dynamical simulated annealing
Expression system: Escherichia coli

Quick links

Citations

10 review citations

H-NS: a universal regulator for a dynamic genome.
Dorman CJ. (2004)
9 more

7 mentions without citation

Ancestral zinc-finger bearing protein MucR in alpha-proteobacteria: A novel xenogeneic silencer?
Jiao et al. (2020)
6 more