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![[Figure 6]](rr5233fig6mag.jpg)
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Figure 6
(a) Structure superposition of KsGH184 (ice blue) and the cell-wall-degrading enzyme of the bacteriophage phi29 tail gp13 (PDB entry 3ct5, ligand complex, light brown). Glu41 (corresponding to the catalytic Glu45 in gp13) and Asp66 (superposed on the potentially ligand-stabilizing Gln54 in gp13) are shown as cylinders. Ethylene glycol molecules are shown as cylinders in cyan. (b) Superposition of both KsGH184 and TtGH184 on the catalytic domain of the full-length gp13; its cell-wall-binding domain differs from the SH3-like domain both in sequence and in structure (it was reported to be similar to LytM, a member of the peptidase M23 family; Firczuk et al., 2005  ). The linker between the two domains of gp13 is poorly ordered, with residues 160–165 missing from the model, which reflects its flexibility, similar to the situation seen in the TsGH24 enzyme (Fig. 2). |
![[Figure 6]](rr5233fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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