› 2pei

X-ray diffraction
2.7Å resolution

Crystal structure of selenomethionine-labeled RbcX

Released:
DOI: 10.2210/pdb2pei/pdb
PDB entry 2pei coloured by chain, front view.
PDB entry 2pei coloured by chain, side view.
PDB entry 2pei 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:
  • not assigned
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, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 109 amino acids
Theoretical weight: 12.85 KDa
Source organism: Synechococcus sp. PCC 7002
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q44177 (Residues: 1-109; Coverage: 81%)
Gene names: SYNPCC7002_A1797, orf134, rbcX
Sequence domains: RbcX protein
Structure domains: Chaperonin-like RbcX

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 48 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P1
Unit cell:
a: 70.362Å b: 71.102Å c: 113.162Å
α: 89.58° β: 81.1° γ: 80.09°
R-values:
R R work R free
0.215 0.212 0.262
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

From chaperonins to Rubisco assembly and metabolic repair.
Hayer-Hartl M. (2017)
2 more