› 3hyb

X-ray diffraction
2.3Å resolution

Crystal structure of RbcX from Anabaena, crystal form II

Released:
DOI: 10.2210/pdb3hyb/pdb
PDB entry 3hyb coloured by chain, front view.
PDB entry 3hyb coloured by chain, side view.
PDB entry 3hyb coloured by chain, top view.
Source organism: Anabaena sp.
Primary publication:
Coupled chaperone action in folding and assembly of hexadecameric Rubisco.
Liu C, Young AL, Starling-Windhof A, Bracher A, Saschenbrecker S, Rao BV, Rao KV, Berninghausen O, Mielke T, Hartl FU, Beckmann R, Hayer-Hartl M
Nature 463 197-202 (2010)
PMID: 20075914

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175014 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RuBisCO chaperone RbcX Chains: A, B
Molecule details ›
Chains: A, B
Length: 155 amino acids
Theoretical weight: 17.69 KDa
Source organism: Anabaena sp.
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q44212 (Residues: 1-135; Coverage: 100%)
Gene name: rbcX
Sequence domains: RbcX protein
Structure domains: Chaperonin-like RbcX

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3121
Unit cell:
a: 74.99Å b: 74.99Å c: 123.841Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.247 0.246 0.275
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

25 review citations

Molecular chaperones in protein folding and proteostasis.
Hartl et al. (2011)
24 more