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![[Figure 3]](rr5231fig3mag.jpg)
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Figure 3
Latch–T3 interface and latch-associated conformational changes in T. maritima reverse gyrase. Structures were superposed onto their H2 domains lacking the latch regions. (a) Cutout of the H2 domain (green), latch regions and the T3 part (red) of the topoisomerase domain. The twisted β-sheet in rgyr_minlatch is colored magenta. An arrow indicates the movement of Phe391 in the β-bulge loop to a location previously occupied by Phe401 of the authentic latch domain. An α-helix (green for wild type and blue for Y851F) rearranges into a loop structure in rgyr_minlatch (magenta). The largest movement is apparent for Tyr364, which flips to the other side (indicated by an arrow). (b) The conformational change in H2 is not due to the β-bulge loop, since it is also observed in structures of the helicase domain with the entire latch removed (indicated by Δ). |
![[Figure 3]](rr5231fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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