Skip to main content
. Author manuscript; available in PMC: 2009 Apr 1.
Published in final edited form as: Bioorg Chem. 2007 Dec 21;36(2):85–90. doi: 10.1016/j.bioorg.2007.11.001

Figure 3.

Figure 3

a) Backbone structure of mtFabH homodimer (subunits in gold and magenta ribbon) in complex with C10S- (space filling) covalently linked to the sidechain sulfur of Cys112 (also space filling) in both subunits. CoASH is shown bound in only the A-subunit (gold), also in space filling model.

b) Semi-transparent surface figure of the mtFabH homodimer rotated slightly about the x-axis relative to A. Subunits are gold and light gray, C10S- and CoASH are green space filling and shown bound in only one subunit. The C10S- group in the acyl channel is completely buried (partly obscured by semi-transparent protein surface envelope); the distal end of the CoASH pantetheinate is buried, while the adenosine pyrophosphate end is exposed at the mouth of the pantetheinate binding channel.