Skip to main content
. Author manuscript; available in PMC: 2013 Apr 1.
Published in final edited form as: Nat Struct Mol Biol. 2009 Dec 13;17(1):31–37. doi: 10.1038/nsmb.1740

Figure 3.

Figure 3

Different configurations of the Ω loop that connects TM2a and TM3 in different FocA monomers, both from the low-formate structure. (a) Structure of Monomer A overlaid with the Ω loop from Monomer E. The Ω loop is colored purple in Monomer A and orange in Monomer E. (b) Close up view of the Ω loop including TM2b in the UP position in Monomer A. (c) Identical view of the Ω loop in the DOWN position in Monomer E. The TM2b helix is at difference positions between the two monomers in both physical space and in sequence. The helices 6 and 4 are removed for clarity. The pore in the center of the monomer as computed by the program HOLE 47 is shown for reference. The structures of Monomers B and C are the same as Monomer A, whereas the structure of Monomer D is similar to that of Monomer E.