› 3qyx

X-ray diffraction
3.75Å resolution

Crystal structure of Mycobacterium tuberculosis EspR in complex with a small DNA fragment

Released:
DOI: 10.2210/pdb3qyx/pdb
PDB entry 3qyx coloured by chain, front view.
PDB entry 3qyx coloured by chain, side view.
PDB entry 3qyx coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Atypical DNA recognition mechanism used by the EspR virulence regulator of Mycobacterium tuberculosis.
Blasco B, Stenta M, Alonso-Sarduy L, Dietler G, Peraro MD, Cole ST, Pojer F
Mol Microbiol 82 251-64 (2011)
PMID: 21883526

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-116791 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Nucleoid-associated protein EspR Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 133 amino acids
Theoretical weight: 14.74 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WJB7 (Residues: 2-132; Coverage: 99%)
Gene names: Rv3849, espR
Structure domains: lambda repressor-like DNA-binding domains
5'-D(*A*CP*GP*CP*CP*GP*AP*AP*TP*C)-3' Chain: E
Molecule details ›
Chain: E
Length: 10 nucleotides
Theoretical weight: 3.01 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P32
Unit cell:
a: 86.955Å b: 86.955Å c: 130.363Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.206 0.235
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

2 review citations

Evolutionary landscape of the Mycobacterium tuberculosis complex from the viewpoint of PhoPR: implications for virulence regulation and application to vaccine development.
Broset et al. (2015)
1 more

2 mentions without citation

A single aromatic core mutation converts a designed "primitive" protein from halophile to mesophile folding.
Longo et al. (2015)
1 more