 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](wd5223fig1mag.jpg)
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Figure 1
Structural features of Af Cmr1. (a) Folding topology. Af Cmr1 is composed of N- and C-terminal ferredoxin-like domains (N-FLD and C-FLD), each of which contains the signature topology βαββαβ shown in violet and blue, respectively. (b) Two views of the structure. The secondary-structural elements are numbered in the order of their appearance in the primary sequence. The disordered segments are indicated by dotted lines and the flanking residues are labelled. Their predicted secondary structures and disorder scores are tabulated. (c) Structural similarity to Cas6. The structures of Af Cmr1 and Cas6 are superimposed. Only the N-terminal FLDs can be superposed. Compared with the N-FLD of Cas6, that of Af Cmr1 contains an extra α-helix (α4), which interacts with both the N-terminal and the C-terminal FLDs. The RNA molecule bound to Cas6 is shown in orange. |
![[Figure 1]](wd5223fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
