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![[Figure 6]](rr5231fig6mag.jpg)
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Figure 6
The different shapes, sizes and electrostatic surface potentials of latch domains. The vertical line separates the AF2 models (right) from the crystallographic structures (left). A superposition of all structures and models on their H2 domains is shown at the lower left. The sequences of the two β-hairpin-forming β-strands are given with the number of residues forming the rest of the latch in between. Ribbon representations are to scale and in the same orientation as in the superposition. Surfaces of latch domains are rotated by 90° about the x axis to provide a top view of the latch with the right-hand side pointing towards the T3 region of the topoisomerase domains. A region of positive electrostatic potential is apparent on the right-hand side of several, but not all, latch domains. Crystal structures are A.fu, A. fulgidus; T.ma., T. maritima; ml, rgyr_minlatch from T. maritima. AF2 models are T.af., T. africanus (UniProt B7IEV8); ml, T.ma., rgyr_minlatch; C.te., C. subterraneus subsp. tengcongensis (Q8R979); S.so., S. solfataricus (Q97ZZ8); S.to., S. tokodaii (Q971T7); P.ca., P. calidifontis (A3MU01); D.am., D. amylolyticus (B8D628); P.fu., P. furiosus (P95479). |
![[Figure 6]](rr5231fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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