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![[Figure 9]](yt5100fig9mag.jpg)
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Figure 9
The lateral site of Aae Hfq is pre-structured for RNA binding. The three-dimensional structure of the single, unique monomer from the Hfq-U6 co-crystal structure (teal backbone) was superimposed with the 12 subunits of the apo Hfq structure (grey). Residues that contact RNA, to within ∼3.6 Å in the P6 Hfq·U6 structure, are shown as sticks for both the P6 and P1 structures. Apart from residue Glu7, which sterically occludes the binding pocket and thus is likely to adopt a different conformation upon RNA binding, note that the side chains in the apo structure adopt rotameric states quite similar to those in the three-dimensional structure of U6-bound Aae Hfq. This finding suggests pre-organization of the RNA-binding site of Aae Hfq. |
![[Figure 9]](yt5100fig9.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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