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. Author manuscript; available in PMC: 2016 Mar 17.
Published in final edited form as: Biochemistry. 2015 Mar 3;54(10):1943–1955. doi: 10.1021/bi5014358

Figure 6.

Figure 6

Interpretation of the ecFabI-ACP complex structure. (A) Symmetry-related ecFabI homo-tetramer (gray) within the ecFabI-NAD+-DD-ACP structure (yellow, PDB-code: 2FHS; two FabI monomers and one ACP in the asymmetric unit). The partial ACP model is depicted in cyan. (B) ACP environment in the 2FHS-structure. To derive a full ACP model, decanoyl-ecACP (lilac, PDB-code: 2FAE) was superimposed onto the partial ACP model of the 2FHS-structure considering only main chain atoms. (C) Superposition of the two crystallographically feasible FabI-ACP interaction models. The originally proposed model is depicted in yellow, the model derived from the interaction with a symmetry related FabI monomer is colored in gray. (D, E) FabI-ACP clash-test. The simultaneous interaction of the FabI homo-tetramer with four ACP substrates will lead to severe clashes for the original model (highlighted in red; panel D) 11, whereas no clashes are observed for the new model (panel E). These figures were created by superimposing both models (panel C) on each subunit of the full FabI homo-tetramer.