4LWO

Crystal structure of PRMT6

Summary for 4LWO

• Entry DOI: 10.2210/pdb4lwo/pdb
• Related: 4LWP
• Descriptor: Arginine N-methyltransferase, putative (2 entities in total)
• Functional Keywords: sam binding domain, arginine methylation, transferase
• Biological source: Trypanosoma brucei brucei
• Total number of polymer chains: 4
• Total formula weight: 165029.86

Authors

Zhu, Y.,Wang, C.,Shi, Y.,Teng, M. (deposition date: 2013-07-28, release date: 2014-02-19, Last modification date: 2024-03-20)

Primary citation

Wang, C.,Zhu, Y.,Chen, J.,Li, X.,Peng, J.,Chen, J.,Zou, Y.,Zhang, Z.,Jin, H.,Yang, P.,Wu, J.,Niu, L.,Gong, Q.,Teng, M.,Shi, Y.
Crystal Structure of Arginine Methyltransferase 6 from Trypanosoma brucei
Plos One, 9:e87267-e87267, 2014

PubMed Abstract: Arginine methylation plays vital roles in the cellular functions of the protozoan Trypanosoma brucei. The T. brucei arginine methyltransferase 6 (TbPRMT6) is a type I arginine methyltransferase homologous to human PRMT6. In this study, we report the crystal structures of apo-TbPRMT6 and its complex with the reaction product S-adenosyl-homocysteine (SAH). The structure of apo-TbPRMT6 displays several features that are different from those of type I PRMTs that were structurally characterized previously, including four stretches of insertion, the absence of strand β15, and a distinct dimerization arm. The comparison of the apo-TbPRMT6 and SAH-TbPRMT6 structures revealed the fine rearrangements in the active site upon SAH binding. The isothermal titration calorimetry results demonstrated that SAH binding greatly increases the affinity of TbPRMT6 to a substrate peptide derived from bovine histone H4. The western blotting and mass spectrometry results revealed that TbPRMT6 methylates bovine histone H4 tail at arginine 3 but cannot methylate several T. brucei histone tails. In summary, our results highlight the structural differences between TbPRMT6 and other type I PRMTs and reveal that the active site rearrangement upon SAH binding is important for the substrate binding of TbPRMT6.

PubMed: 24498306
DOI: 10.1371/journal.pone.0087267

Experimental method

X-RAY DIFFRACTION (2.203 Å)