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. 2018 Mar 8;13(3):e0193205. doi: 10.1371/journal.pone.0193205

Fig 3. Structures of PRMT5 and the PRMT5:MEP50 complex.

Fig 3

(A) An individual PRMT5 subunit from Protein Databank Entry 4GQB is represented as a ribbon diagram with dehydrosinefungin (white C atoms) and a histone H4 derived peptide (yellow C atoms) depicted as CPK spheres. The TIM barrel domain, Rossmann fold and β-barrel domains are colored blue, red and green, respectively. (B) The 3D reconstruction of the PRMT5:MEP50 complex, viewed along a dyad axis, is represented as a transparent gray map contoured at 3 rmsd (0.036). The PRMT5 subunits (colored as in Fig 3A) and the MEP50 subunits (colored magenta) were rigid body fit within the map as heterodimeric units. Black arrows highlight weak or missing density for PRMT5 residues 173–179. Density for loop residues 488–493 is highlighted by stars. Views of the 3D reconstruction along the other two central dyad axes are available in S3 Fig. (C) A resolution of 3.7 Å for the reconstruction is indicated at FSC = 0.143.