› 1uw9

X-ray diffraction
2.05Å resolution

L290F-A222T chlamydomonas Rubisco mutant

Released:
DOI: 10.2210/pdb1uw9/pdb
PDB entry 1uw9 coloured by chain, front view.
PDB entry 1uw9 coloured by chain, side view.
PDB entry 1uw9 coloured by chain, top view.
Source organism: Chlamydomonas reinhardtii
Primary publication:
Altered intersubunit interactions in crystal structures of catalytically compromised ribulose-1,5-bisphosphate carboxylase/oxygenase.
Karkehabadi S, Taylor TC, Spreitzer RJ, Andersson I
Biochemistry 44 113-20 (2005)
PMID: 15628851

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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero hexadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133651 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ribulose bisphosphate carboxylase large chain Chains: A, B, E, H, K, O, R, V
Molecule details ›
Chains: A, B, E, H, K, O, R, V
Length: 475 amino acids
Theoretical weight: 52.76 KDa
Source organism: Chlamydomonas reinhardtii
UniProt:
  • Canonical: P00877 (Residues: 1-475; Coverage: 100%)
Gene name: rbcL
Sequence domains:
Structure domains:
Ribulose bisphosphate carboxylase small subunit, chloroplastic 1 Chains: C, F, I, J, M, P, T, W
Molecule details ›
Chains: C, F, I, J, M, P, T, W
Length: 140 amino acids
Theoretical weight: 16.29 KDa
Source organism: Chlamydomonas reinhardtii
UniProt:
  • Canonical: P00873 (Residues: 46-185; Coverage: 76%)
Gene names: CHLREDRAFT_82986, CHLRE_02g120100v5, RBCS-1, RBCS1
Sequence domains: Ribulose bisphosphate carboxylase, small chain
Structure domains: Ribulose bisphosphate carboxylase, small subunit

Ligands and Environments

3 bound ligands:
Ligand MG 8 x MG
Ligand CAP 8 x CAP
Ligand EDO 55 x EDO
3 modified residues:
Ligand HYP 16 x HYP
Ligand KCX 8 x KCX
Ligand SMC 16 x SMC

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 126.073Å b: 178.196Å c: 120.463Å
α: 90° β: 120.35° γ: 90°
R-values:
R R work R free
0.157 0.157 0.194

Quick links

Citations

3 review citations

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

2 mentions without citation

Correlation between amino acid residues converted by RNA editing and functional residues in protein three-dimensional structures in plant organelles.
Yura et al. (2008)
1 more