 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](dw5066fig1mag.jpg)
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Figure 1
Function of Fbxo7 and structure of its FP domain. (a) Function of Fbxo7 as the substrate-recognition component of the SCFFbxo7 E3 ligase. (b) Schematic representation of the putative domains of human Fbxo7. Ubl, ubiquitin-like domain; cdk, Cdk6-interacting motif; FP, Fbxo7/PI31 domain; PRR, proline-rich region. (c) Structure-based sequence alignment of the sequences of the FP domains of Fbxo7 and PI31. Identical and similar residues are highlighted with red and blue backgrounds, respectively. The secondary structures are indicated above and below the sequence for Fbxo7 and PI31, respectively. The α5 helix in the FP domain of Fbxo7 has a kink in the middle denoted by a triangle. The underlined C-terminal sequences are present in the protein constructs used for crystallization, but no electron density was observed for these residues. Note that the protein constructs contain more residues than the putative FP domain as indicated in (b). (d) Overall structure of the FP domain of Fbxo7 colour-ramped from blue at the N-terminus to red at the C-terminus. The crystallization protein contains an artificial N-terminal sequence GPSSP as the result of a cloning artefact (grey). (e) Superimposition of the structures of the FP domains of Fbxo7 (red) and PI31 (blue). |
![[Figure 1]](dw5066fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
