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![[Figure 6]](ni5011fig6mag.jpg)
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Figure 6
Modeling VanRSc assembly on DNA. (a) The activated VanRSc dimer shown in two orthogonal views. The receiver domain is colored cyan, the DNA-binding domain is colored slate blue and the recognition helix α8 is colored hot pink. The positions of the two symmetry-related copies of helix α5 are indicated. (b) To determine whether a head-to-tail configuration was consistent with the structure of activated VanRSc, the VanRSc protomer (purple) was superposed upon each protomer of DNA-bound PmrA (light orange) by aligning the DNA-binding domains. For clarity, the only structural elements shown from the receiver domain are the α5 helices. (c, d) The DNA-binding domain in inactive VanRSc adopts a conformation that is consistent with DNA binding. The DNA-binding domain from inactive VanRSc (red) was superposed upon the corresponding domain from DNA-bound PmrA (light orange). (c) shows this superposition, while (d) shows a surface representation of VanRSc. Both panels reveal that in this pose the VanRSc DNA-binding domain does not clash with the DNA. The PmrA structure was taken from PDB entry 4s04. |
![[Figure 6]](ni5011fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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