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![[Figure 2]](dw5208fig2mag.jpg)
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Figure 2
Crystallographic structure of the ClpC1-NTD–ECU complex. (a) Overall view of the asymmetric unit containing 12 molecules of ClpC1-NTD and 24 molecules of ECU in a 1:2 complex. (b) Initial 2Fo − Fc electron density for ECU showing the quality of the density (2.5 Å) and the intradomain dyad relating ECU site 1 and ECU site 2. (c) Two-dimensional drawing of ECU with each amino-acid carbon labeled in blue. Stereochemical details can be found in Gao et al. (2014  ). Note the depsipeptide linkage between the C-terminus of Val13 and the OH group of Thr4. (d) The structure of the ClpC1-NTD–ECU monomer with known resistance sites highlighted. The sites in pink confer resistance to ECU, while those in aqua confer resistance to RUF-I (Gao et al., 2015; Choules et al., 2019). (e) Refined 2Fo − Fc electron density of ECU site 1 shows unambiguous density for the entire ligand. The tail of ECU1 wraps around, forming an `elbow'-like pocket, and is anchored by the N-terminus of ClpC1-NTD hydrogen-bonding to the C=O of Val2 in ECU1. Four N-methyl groups are highlighted with red circles to emphasize the hydrophobic (upper, curved) versus hydrophilic (lower, straight) surfaces of the ECU molecule. The intradomain dyad relating the two ECU molecules is approximately vertical and in the plane of the figure in (d), between the two ECU molecules; the dyad is perpendicular to the plane of the image and is marked by a yellow oval in (e). |
![[Figure 2]](dw5208fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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