› 1geh

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF ARCHAEAL RUBISCO (RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE)

Released:
DOI: 10.2210/pdb1geh/pdb
PDB entry 1geh coloured by chain, front view.
PDB entry 1geh coloured by chain, side view.
PDB entry 1geh coloured by chain, top view.
Source organism: Thermococcus kodakarensis KOD1
Primary publication:
Crystal structure of a novel-type archaeal rubisco with pentagonal symmetry.
Kitano K, Maeda N, Fukui T, Atomi H, Imanaka T, Miki K
Structure 9 473-81 (2001)
PMID: 11435112

Function and Biology Details

Reaction catalysed: 
2 3-phospho-D-glycerate + 2 H(+) = D-ribulose 1,5-bisphosphate + CO(2) + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131673 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribulose bisphosphate carboxylase Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 444 amino acids
Theoretical weight: 49.78 KDa
Source organism: Thermococcus kodakarensis KOD1
Expression system: Escherichia coli
UniProt:
  • Canonical: O93627 (Residues: 1-444; Coverage: 100%)
Gene names: TK2290, rbc, rbcL
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 10 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P3121
Unit cell:
a: 233.75Å b: 233.75Å c: 93.26Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.224 0.254
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Structure and function of Rubisco.
Andersson et al. (2008)
14 more

7 mentions without citation

Function, structure, and evolution of the RubisCO-like proteins and their RubisCO homologs.
Tabita et al. (2007)
6 more