 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](no5082fig2mag.jpg)
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Figure 2
Details of the Mre11CD crystal structure from C. thermophilum. (a) Detailed view of the CtMre11CD dimer interface consisting of α-helices α2 and α3 from each protomer. (b) CtMre11CD nuclease active site with two coordinated manganese ions (cyan). (c) Overlay of SpMre11CD (grey), SpMre11CD–Nbs1 (light blue) and CtMre11CD (deep blue) by alignment of the nuclease domains onto the nuclease domain of CtMre11CD indicates the movement of the capping domain by up to 5 Å. (d) Fully modelled eukaryotic insertion loop (lime and brown). The interaction between Arg77 and Phe102 is highlighted. Selected residues are depicted as colour-coded sticks and annotated. Hydrogen bonds in (a) and (d) are highlighted as dashed lines. |
![[Figure 2]](no5082fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
