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Figure 3
Inter-domain interactions of the FP domain of Fbxo7. (a) Two adjacent FP domains in the crystals interact with each other through the α-helical interface in one domain (in purple) and the β-­stranded interface (in blue). The shown structures do not contain the N- and C-terminal loops. The structures are rendered in surface mode (with 20% transparency) and cartoon mode. (b) Hydrogen bonds in the domain–domain interface. The residues involved in the hydrogen bonds are shown as sticks. The view is identical to that in (a). (c) The 2FoFc electron-density map contoured at 1σ is shown for several residues (shown as sticks) in the domain–domain interface. (d) Hydrophobic interactions in the domain–domain interface. The two interacting FP domains are rendered in surface mode (coloured by element, with C, N and O atoms in green, blue and red, respectively) and cartoon mode (coloured magenta), respectively. The residues involved in the hydrophobic interactions are indicated in two different ways for the two protomers: on the molecular surface with red/italic residue names and as sticks (coloured in cyan) with black residue names. The inter-domain interface is the same in the two different crystal forms.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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