› 2peq

X-ray diffraction
1.9Å resolution

Crystal structure of RbcX, crystal form II

Released:
DOI: 10.2210/pdb2peq/pdb
PDB entry 2peq coloured by chain, front view.
PDB entry 2peq coloured by chain, side view.
PDB entry 2peq coloured by chain, top view.
Source organism: Synechococcus sp. PCC 7002
Primary publication:
Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco.
Saschenbrecker S, Bracher A, Rao KV, Rao BV, Hartl FU, Hayer-Hartl M
Cell 129 1189-200 (2007)
PMID: 17574029

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175010 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RuBisCO chaperone RbcX Chains: A, B
Molecule details ›
Chains: A, B
Length: 134 amino acids
Theoretical weight: 15.28 KDa
Source organism: Synechococcus sp. PCC 7002
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q44177 (Residues: 1-134; Coverage: 100%)
Gene names: SYNPCC7002_A1797, orf134, rbcX
Sequence domains: RbcX protein
Structure domains: Chaperonin-like RbcX

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: I222
Unit cell:
a: 63.505Å b: 69.339Å c: 98.795Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.197 0.253
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

Converging concepts of protein folding in vitro and in vivo.
Hartl et al. (2009)
17 more

3 mentions without citation

Structure of the RuBisCO chaperone RbcX from the thermophilic cyanobacterium Thermosynechococcus elongatus.
Tarnawski et al. (2011)
2 more