Figure 2. Crystal structure of the fusion protein EntE-B.

A. Ribbon representation of the 10 protein chains present in the asymmetric unit. Each chain is shown in a different color with functionally interacting subunits shown in similar colors. B. Electron density of the active site for Chain C EntE molecule. Unbiased electron density with coefficients of the form F_o-F_c calculated prior to inclusion of ligands is shown. The density is contoured at 3σ, centered on atom C5P of the pantetheine chain, and shown as a sphere with radius 12Å. C. Ribbon representation of the functional interaction between EntE and the EntB carrier protein domain. The N-terminal domain of EntE is shown with blue helices and purple sheets while the C-terminal domain is shown in green. The carrier domain is shown in red. The pantetheine cofactor and inhibitor are shown in stick representation with yellow, red, blue, orange, and gold for carbon, oxygen, nitrogen, phosphorus, and sulfur, respectively. D. Two complete chains of the interacting dimer in green and blue. The EntE domain is shown in surface representation and the PCP domain and C-terminal helix of EntE are shown as ribbons. E. Stereorepresentation of the active site of EntE (in blue) with EntB shown in red. The cofactor and inhibitor are shown in ball-and-stick representation, colored as in panel A. Panels B and E are shown in the same orientation. See also Figure S2 for a comparison of the multiple copies in the asymmetric unit.