› 3i59

X-ray diffraction
2.29Å resolution

Crystal structure of MtbCRP in complex with N6-cAMP

Released:
DOI: 10.2210/pdb3i59/pdb
PDB entry 3i59 coloured by chain, front view.
PDB entry 3i59 coloured by chain, side view.
PDB entry 3i59 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Structural insights into the mechanism of the allosteric transitions of Mycobacterium tuberculosis cAMP receptor protein.
Reddy MCM, Palaninathan SK, Bruning JB, Thurman C, Smith D, Sacchettini JC
J Biol Chem 284 36581-36591 (2009)
PMID: 19740754

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161792 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
CRP-like cAMP-activated global transcriptional regulator Chain: A
Molecule details ›
Chain: A
Length: 249 amino acids
Theoretical weight: 27.64 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WMH3 (Residues: 1-224; Coverage: 100%)
Gene names: Rv3676, crp
Sequence domains:
Structure domains:
CRP-like cAMP-activated global transcriptional regulator Chain: B
Molecule details ›
Chain: B
Length: 249 amino acids
Theoretical weight: 27.6 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WMH3 (Residues: 1-224; Coverage: 100%)
Gene names: Rv3676, crp
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand N6R 1 x N6R
Ligand CL 1 x CL
Ligand N6S 1 x N6S
1 modified residue:
Ligand MSE 1 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: C2
Unit cell:
a: 113.732Å b: 75.716Å c: 63.639Å
α: 90° β: 110.91° γ: 90°
R-values:
R R work R free
0.234 0.234 0.284
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Cyclic-AMP and bacterial cyclic-AMP receptor proteins revisited: adaptation for different ecological niches.
Green et al. (2014)
3 more

3 mentions without citation

cAMP-regulated protein lysine acetylases in mycobacteria.
Nambi et al. (2010)
2 more