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![[Figure 1]](ys5009fig1mag.jpg)
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Figure 1
Schematic model of the full-length ClpX hexamer. A monomeric model of the ATPase domain of E. coli ClpX has been generated with that of H. pylori ClpX [Protein Data Bank (PDB) ID: 1UM8] using the SWISS-MODEL server (Schwede et al., 2003  ) initially. The hexameric model has been generated with the guidance of HslU hexamer (PDB ID: 1E94), and the resulting model was energetically minimized using CNS software (Brunger et al., 1998). Although the exact orientation of ZBD is ambiguous, their location is distal to the ATPase domain (AAA+ ring) of ClpX based on earlier electron microscopic images (Grimaud et al., 1998), as well as the direction of each chain terminus (N-terminus for the polypeptide chain of ATPase domain and C-terminus for that of ZBD). (a) Top view showing the hexameric pore in the center. The ZBD is drawn with ribbon and the ATPase domain (AAA) with ribbon plus transparent molecular surface, and the linker between the ATPase domain and ZBD is missing. (b) Side view [90° rotation of (a) along the horizontal axis] with the ZBD domain extending upward. The figure was drawn using PyMOL (https://www.pymol.org). |
![[Figure 1]](ys5009fig1.jpg)
 | JOURNAL OF SYNCHROTRON RADIATION |
ISSN: 1600-5775
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