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![[Figure 1]](jb5063fig1mag.jpg)
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Figure 1
(a) MtbESX-5 model based on reported cryo-EM structures, showing the proposed conformational alteration of EccC5 between an open/extended conformation (left) and a close/contracted conformation (right). (b) Domain architecture of EccC5 consisting of the transmembrane (yellow), stalk (grey) and DUF (green) domains followed by three ATPase domains, D1, D2 and D3 (top), where the DUF and D1–D3 domains are interconnected by connectors referred to as Linker1, Linker2 and Linker3. (c) Superimposition of the SrsEssCD3 crystal structure (PDB entry 6vt1, blue) with cryo-EM models of ![[Mtb{\rm EccC_5^{DUF}}]](teximages/jb5063fi4.svg){kind=small} (PDB entry 7npr, dark grey), ![[Mxp{\rm EccC_5^{DUF}}]](teximages/jb5063fi5.svg){kind=small} (PDB entry 7b9s, light grey) and ![[Msm{\rm EccC_3^{DUF}}]](teximages/jb5063fi1.svg){kind=small} (PDB entry 6sgx, white) showing the conservation of the overall fold (left) and the similar arrangement of the Walker motifs (right). |
![[Figure 1]](jb5063fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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