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![[Figure 2]](ni5032fig2mag.jpg)
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Figure 2
Ribbon representation of AlphaFold-predicted models of Dpo31. The different domains from D1 to D4 are labeled. (a) Prediction of full-length Dpo31 when submitting the sequence as a monomer, without specifying the oligomeric state, resulting in a curved overall shape. (b) Superimposition of the AlphaFold-predicted model (yellow), when specifying the oligomeric state as a trimer, onto the crystal structure of Dpo31 (the three monomers are colored magenta, cyan and green, respectively). D4 is absent in the crystal structure and D3 of both models fits well, but the presence of a clear twist or rotation, starting from D2 and increasing towards D1, results in a large discrepancy between these domains in the predicted and experimental structures. |
![[Figure 2]](ni5032fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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