2h2j

X-ray diffraction
2.45Å resolution

Structure of Rubisco LSMT bound to Sinefungin and Monomethyllysine

Released:

Function and Biology Details

Reactions catalysed:
3 S-adenosyl-L-methionine + [ribulose-bisphosphate carboxylase]-L-lysine = 3 S-adenosyl-L-homocysteine + [ribulose-bisphosphate carboxylase]-N(6),N(6),N(6)-trimethyl-L-lysine
3 S-adenosyl-L-methionine + [fructose-bisphosphate aldolase]-L-lysine = 3 S-adenosyl-L-homocysteine + [fructose-bisphosphate aldolase]-N(6),N(6),N(6)-trimethyl-L-lysine

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
homo dimer
PDBe Complex ID:
PDB-CPX-174981 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 440 amino acids
Theoretical weight: 50.17 KDa
Source organism: Pisum sativum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q43088 (Residues: 49-482; Coverage: 89%)
Gene name: RBCMT
Sequence domains: Rubisco LSMT substrate-binding
Structure domains:

Ligands and Environments


Cofactor: Ligand SFG 3 x SFG
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: I222
Unit cell:
a: 132.37Å b: 156.5Å c: 267.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.253 0.253 0.292
Expression system: Escherichia coli BL21(DE3)