› 5bqt

X-ray diffraction
3Å resolution

Structure of TrmBL2, an archaeal chromatin protein, shows a novel mode of DNA binding.

Released:
DOI: 10.2210/pdb5bqt/pdb
PDB entry 5bqt coloured by chain, front view.
PDB entry 5bqt coloured by chain, side view.
PDB entry 5bqt coloured by chain, top view.
Source organism: Pyrococcus furiosus
Primary publication:
Structural Insights into Nonspecific Binding of DNA by TrmBL2, an Archaeal Chromatin Protein.
Ahmad MUD, Waege I, Hausner W, Thomm M, Boos W, Diederichs K, Welte W
J Mol Biol 427 3216-3229 (2015)
PMID: 26299937

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186458 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative HTH-type transcriptional regulator TrmBL2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 262 amino acids
Theoretical weight: 30.42 KDa
Source organism: Pyrococcus furiosus
UniProt:
  • Canonical: Q8U3H1 (Residues: 2-263; Coverage: 99%)
Gene names: PF0496, trmBL2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P21212
Unit cell:
a: 82.298Å b: 235.143Å c: 63.511Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.233 0.289

Quick links

Citations

4 review citations

Protocols for Molecular Modeling with Rosetta3 and RosettaScripts.
Bender et al. (2016)
3 more

1 mention without citation

In-Cell Enzymology To Probe His-Heme Ligation in Heme Oxygenase Catalysis.
Sigala et al. (2016)