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![[Figure 7]](dw5208fig7mag.jpg)
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Figure 7
Quaternary-structural insights from comparison of B. subtilis ClpC–MecA and MtbClpC1-NTD–ECU structures. (a) The ClpC hexamer from B. subtilis (PDB entry 3j3s) is shown in gray; one monomer is in color. MtbClpC1-NTD–ECU can be seen in beige with ECU molecules as spheres at the NTD–D1 interface. (b) A single monomer from PDB entry 3j3s is shown with each domain in a different shade of purple. ClpC1-NTD–ECU is in beige with ECU site 1 in cornflower blue and ECU site 2 in cyan. The binding site of the bound MecA is shown in yellow (MecA was removed for simplicity). A longer linker loop (green) connects the NTD to domain D1. The ATP-binding regions (Walker A and B) in domains D1 and D2 are colored orange. (c) ECU site 1 (cornflower blue) occupies the space at the beginning of the Walker A region (orange). The ECU-resistance sites Leu92 and Leu96 are in pink; Leu96 is in the foreground. The atoms of ECU1 overlap with the D1 domain. |
![[Figure 7]](dw5208fig7.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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