Figure 1 - full size

 

Figure 1.
Figure 1: Structure of the VPS29–VPS35 subcomplex. a, VPS29 is green and VPS35 red. b, The surface of VPS35 is shown, with the residues blocking the metallophosphoesterase site of VPS29 in grey, and other residues that contact VPS29 in purple. c, The surface of VPS29 is shown, with residues surrounding the metallophosphoesterase site in light blue, and other VPS35-contacting residues in purple. d, Hydrophobic grooves on the outer surface of VPS35 are formed between even-numbered helices. The probability of the surface to participate in ligand binding was coloured from lowest to highest in a blue to red gradient using the hotpatch server (http://hotpatch.mbi.ucla.edu/). Structural figures were generated with pymol (http://www.pymol.org/).

The above figure is reprinted by permission from Macmillan Publishers Ltd: Nature (2007, 449, 1063-1067) copyright 2007.