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. Author manuscript; available in PMC: 2011 Jan 12.
Published in final edited form as: Biochemistry. 2010 Jan 12;49(1):236–246. doi: 10.1021/bi901725x

FIGURE 4. Comparison of the dimer structures of sCD-MPR in the absence and presence of Man-6-P with that of EQKM/Man-6-P.

FIGURE 4

(A) The Man-6-P bound structure of EQKM (3K41, blue/grey) was overlayed (B) with the structures of sCD-MPR crystallized in the unbound state (2RL7, grey/yellow) as well as bound to Man-6-P (2RL8, magenta/pink). (C) and (D), The dimers have been rotated down 90° from the view in (A) and (B), showing the superimposition looking down the Z axis. Close-up view showing the dimer interface of (E) EQKM/Man-6-P (3K41) and (F) sCD-MPR (2RL8). Residues on loop D proposed to interact with either the ligand or loop N of the other monomer are shown. Black dashed lines indicate potential hydrogen bond or salt bridge interactions. Loops C and D are indicated in panels A, C, E and F. The N- and C-terminus are boxed in panels A, C and D. The location of Man-6-P (yellow ball-and-stick) is shown.