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![[Figure 1]](rr5231fig1mag.jpg)
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Figure 1
Domain organization and active site in reverse gyrases. (a) Structure of T. maritima wild-type reverse gyrase (PDB entry 4ddu) colored according to the subdomains present in reverse gyrases. The right-hand side maps the domains onto the sequence, showing that some subdomains are inserts in larger domains. The H1 and H2 domains are RecA-like folds that constitute the helicase domain. The latch (orange) is an insert in the H2 domain and `latches' against the topoisomerase domain (red). It is a short, two-stranded β-sheet with a globular, helical domain inserted at its tip. The topoisomerase domain harbors the catalytic tyrosine (Tyr851 in T. maritima). It is subdivided into four regions termed T1–T4 (boxed). (b) The Y851F variant (blue) has little effect on the structure of the active site. The plasticity between the wild-type structures PDB entries 4ddu (red) and 4ddt (gray) is on the same scale as that on comparison with the Y851F variant. Hence, the Y851F variant structure can be included in the group of structures for an unbiased comparison with rgyr_minlatch. |
![[Figure 1]](rr5231fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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