› 3jsp

X-ray diffraction
2.9Å resolution

Classic Protein With a New Twist: crystal structure of a LexA repressor DNA complex

Released:
DOI: 10.2210/pdb3jsp/pdb
PDB entry 3jsp coloured by chain, front view.
PDB entry 3jsp coloured by chain, side view.
PDB entry 3jsp coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structure of the LexA-DNA complex and implications for SOS box measurement.
Zhang AP, Pigli YZ, Rice PA
Nature 466 883-6 (2010)
PMID: 20703307

Function and Biology Details

Reaction catalysed: 
Hydrolysis of Ala(84)-|-Gly bond in repressor LexA.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-116451 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
LexA repressor Chains: A, B
Molecule details ›
Chains: A, B
Length: 202 amino acids
Theoretical weight: 22.33 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A7C2 (Residues: 1-202; Coverage: 100%)
Gene names: JW4003, b4043, exrA, lexA, spr, tsl, umuA
Sequence domains:
Structure domains:
DNA (5'-D(*TP*AP*TP*AP*CP*TP*GP*TP*AP*TP*GP*CP*GP*CP*AP*TP*AP*CP*AP*GP*TP*A)-3') Chains: C, D
Molecule details ›
Chains: C, D
Length: 22 nucleotides
Theoretical weight: 6.75 KDa
Source organism: Escherichia coli K-12
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21212
Unit cell:
a: 94.193Å b: 116.869Å c: 66.477Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.267 0.266 0.287
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

9 review citations

SOS, the formidable strategy of bacteria against aggressions.
Baharoglu et al. (2014)
8 more

3 mentions without citation

Lipid-dependent sequential allosteric activation of heat-sensing TRPV1 channels by anchor-stereoselective "hot" vanilloid compounds and analogs.
Wang G. (2021)
2 more