› 1l5y

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF MG2+ / BEF3-BOUND RECEIVER DOMAIN OF SINORHIZOBIUM MELILOTI DCTD

Released:
DOI: 10.2210/pdb1l5y/pdb
PDB entry 1l5y coloured by chain, front view.
PDB entry 1l5y coloured by chain, side view.
PDB entry 1l5y coloured by chain, top view.
Source organism: Sinorhizobium meliloti
Primary publication:
Two-component signaling in the AAA + ATPase DctD: binding Mg2+ and BeF3- selects between alternate dimeric states of the receiver domain.
Park S, Meyer M, Jones AD, Yennawar HP, Yennawar NH, Nixon BT
FASEB J 16 1964-6 (2002)
PMID: 12368235

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146678 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
C4-dicarboxylate transport transcriptional regulatory protein DctD Chains: A, B
Molecule details ›
Chains: A, B
Length: 155 amino acids
Theoretical weight: 16.82 KDa
Source organism: Sinorhizobium meliloti
Expression system: Escherichia coli
UniProt:
  • Canonical: P13632 (Residues: 2-143; Coverage: 31%)
Gene names: RB1525, SMb20613, dctD
Sequence domains: Response regulator receiver domain
Structure domains: Rossmann fold

Ligands and Environments

6 bound ligands:
Ligand MG 2 x MG
Ligand SO4 4 x SO4
Ligand BEF 3 x BEF
Ligand BF2 10 x BF2
Ligand BF4 1 x BF4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 52.005Å b: 76.837Å c: 77.853Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.229
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Bacterial response regulators: versatile regulatory strategies from common domains.
Gao et al. (2007)
4 more

7 mentions without citation

Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains.
Lee et al. (2003)
6 more