Structure of Rubisco LSMT bound to AdoMet

Catalytic Roles for Carbon-Oxygen Hydrogen Bonding in SET Domain Lysine Methyltransferases.

Ribulose-1,5 bisphosphate carboxylase/oxygenase

[Ribulose- bisphosphate carboxylase]-lysine N-methyltransferase, RuBisCO methyltransferase, RuBisco LSMT, rbcMT

100 mM Bis Tris Propane, pH 6.8, 0.87-1.17 M NaAcetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K

The same enzyme in complex with AdoHcy and HEPES.

The same enzyme in complex with AdoHcy and lysine.

The same enzyme in complex with AdoHcy and monomethyllysine.

The engineered construct possesses an ENLYFQ sequence on its C-terminus due to a TEV protease cleavage site.

Ribulose-1,5 bisphosphate carboxylase/oxygenase (E.C.2.1.1.127)

There are three molecules of LSMT the asymmetric unit. LSMT is a monomer in solution.

SET domain, protein lysine methyltransferase, TRANSFERASE