› 2l92

Solution NMR

Solution structure of the C-terminal domain of H-NS like protein Bv3F

Released:
DOI: 10.2210/pdb2l92/pdb
PDB entry 2l92 coloured by chain, ensemble of 20 models, front view.
PDB entry 2l92 coloured by chain, ensemble of 20 models, side view.
PDB entry 2l92 coloured by chain, ensemble of 20 models, top view.
Source organism: Burkholderia vietnamiensis G4
Primary publication:
Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins.
Gordon BR, Li Y, Cote A, Weirauch MT, Ding P, Hughes TR, Navarre WW, Xia B, Liu J
Proc Natl Acad Sci U S A 108 10690-5 (2011)
PMID: 21673140

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107377 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA-binding protein Bv3F Chain: A
Molecule details ›
Chain: A
Length: 50 amino acids
Theoretical weight: 5.66 KDa
Source organism: Burkholderia vietnamiensis G4
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: A4JS72 (Residues: 71-112; Coverage: 38%)
Gene names: Bcep1808_6219, Bcep1808_7148
Sequence domains: H-NS histone family
Structure domains: H-NS DNA Binding Protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 84%
Refinement method: simulated annealing
Expression system: Escherichia coli BL21

Quick links

Citations

15 review citations

Chromosome organization in bacteria: mechanistic insights into genome structure and function.
Dame et al. (2020)
14 more

1 mention without citation

Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins.
Gordon et al. (2011)