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Figure 1
Crystal structure of uncomplexed FIP2. (a) Crystal packing in a section of the lattice. The asymmetric unit comprising four monomers is shown in identical colors. The monomers begin between residues 445 and 451, while the C-terminus is either residue 496 or 497. (b) The asymmetric unit consists of two pairs of antiparallel α-helices. (c) The NMR structure of uncomplexed FIP2 (residues 449–489) is a parallel dimer that is frayed as the helices extend towards the C-terminus. (d) The crystal structure of FIP2 (residues 448–503) from its complex with Rab11 (not shown). The closely packed parallel dimer has a hook at the C-terminus that is stabilized by hydrophobic packing.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 76| Part 8| August 2020| Pages 357-363
https://doi.org/10.1107/S2053230X20009164
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