Structural characterization and conservation of CsMRP4. a A 3D homology model was built based on the solved structure templates. The α-helix and β-strand are depicted as ribbon diagrams, and coiled-coil is depicted as a line. TM α-helices are colored and numbered from the N-terminus (blue) to the C-terminus (red). The red rectangles indicate the entrance of inner cavity, and spheres correspond to residues coordinating ATP-binding sites. b TM α-helices, as viewed perpendicular to the horizontal plane marked with red arrowheads. c The degree of sequence conservation is colored using a color gradient from white (divergent) to red (conserved). Structural conservation corresponds to the radii of the backbone sausage representation, which is proportional to the root-mean-squared deviation at each position between structure alignments. PDB IDs of the identified homologs are as follows: 5W81_A, 5UAK_A, 5UJ9_A, 4C3Z_A, 2PZG_A, 3GD7_A, 4Q4J_B, 1R0Z_A, 2HYD_A, 4Q7M_B, 4Q4J_A, 5DGX_A, 5IDV_A, 4MYC_A, 3WMF_A, 5MKK_A, 1MV5_A, 4MRN_A, 3NH6_A, 2FFB_A, 5EUM_A, 4F4C_A, 2GHI_A, 5MKK_B, 4Q9H_A, 4AYW_A, 3VX4_A, 5U1D_B, 5U1D_A, 4PL0_A, 5L22_B, 4U00_A, 4K8O_A, 4MKI_B, 4HUQ_B, 3TUJ_C, 5NIK_J, and 5JSZ_A. Structural alignment and image rendering were carried out using ENDscript and PyMOL (See details in the Methods section)