› 1j3l

X-ray diffraction
2.3Å resolution

Structure of the RNA-processing inhibitor RraA from Thermus thermophilis

Released:
DOI: 10.2210/pdb1j3l/pdb
PDB entry 1j3l coloured by chain, front view.
PDB entry 1j3l coloured by chain, side view.
PDB entry 1j3l coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Structure of the RNA-processing inhibitor RraA from Thermus thermophilis.
Rehse PH, Kuroishi C, Tahirov TH
Acta Crystallogr D Biol Crystallogr 60 1997-2002 (2004)
PMID: 15502308

Function and Biology Details

Reactions catalysed: 
Oxaloacetate = pyruvate + CO(2)
2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177970 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-4-methyl-2-oxoglutarate aldolase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 164 amino acids
Theoretical weight: 17.46 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SIP7 (Residues: 1-164; Coverage: 100%)
Gene name: TTHA1322
Sequence domains: Aldolase/RraA
Structure domains: Ribonuclease E inhibitor RraA/RraA-like

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand CL 2 x CL
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: C2221
Unit cell:
a: 61.872Å b: 109.068Å c: 270.319Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.206 0.274
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

The regulatory protein RraA modulates RNA-binding and helicase activities of the E. coli RNA degradosome.
Górna et al. (2010)
3 more

4 mentions without citation

Insight into the Mechanism of Intramolecular Inhibition of the Catalytic Activity of Sirtuin 2 (SIRT2).
Li et al. (2015)
3 more