EMD-1735

Single-particle
11.0 Å
EMD-1735 Deposition: 26/05/2010
Map released: 23/07/2010
Last modified: 16/05/2012
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-1735

Rubisco in complex with Rubisco large subunit methyltransferase

EMD-1735

Single-particle
11.0 Å
EMD-1735 Deposition: 26/05/2010
Map released: 23/07/2010
Last modified: 16/05/2012
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Spinacia oleracea, Pisum sativum
Sample: Spinach RuBisCO in complex with pea RuBisCO LSMT

Deposition Authors: Raunser S , Magnani R, Huang Z, Houtz RL, Trievel RC, Penczek PA, Walz T
Rubisco in complex with Rubisco large subunit methyltransferase.
Raunser S , Magnani R, Huang Z, Houtz RL, Trievel RC, Penczek PA, Walz T
(2009) PNAS , 106 , 3160 - 3165
Abstract:
SET domain protein lysine methyltransferases (PKMT) are a structurally unique class of enzymes that catalyze the specific methylation of lysine residues in a number of different substrates. Especially histone-specific SET domain PKMTs have received widespread attention because of their roles in the regulation of epigenetic gene expression and the development of some cancers. Rubisco large subunit methyltransferase (RLSMT) is a chloroplast-localized SET domain PKMT responsible for the formation of trimethyl-lysine-14 in the large subunit of Rubisco, an essential photosynthetic enzyme. Here, we have used cryoelectron microscopy to produce an 11-A density map of the Rubisco-RLSMT complex. The atomic model of the complex, obtained by fitting crystal structures of Rubisco and RLSMT into the density map, shows that the extensive contact regions between the 2 proteins are mainly mediated by hydrophobic residues and leucine-rich repeats. It further provides insights into potential conformational changes that may occur during substrate binding and catalysis. This study presents the first structural analysis of a SET domain PKMT in complex with its intact polypeptide substrate.