 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](ft5109fig3mag.jpg)
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Figure 3
Comparisons of FIP2 in Rab11-bound and free states. (a) Complex of Rab11 (residues 7–173) with residues 448–503 of FIP2 (PDB entry 4c4p). The effector domain is at the extreme C-terminus of the 512-residue protein. Residues 129–290 of FIP2 (arrows), which lie upstream of the Rab11 effector domain, comprise the myosin Vb-binding region. Following α5 of Rab11, a hypervariable region of 43 residues is prenylated at two cysteine residues near the C-terminus of the 216-residue protein. This flexible region was dispensed with to enable crystallization of the complex (Lall et al., 2013  ). (b) Superposition of chain A of FIP2 with one of the α-helices from the Rab11–FIP2 complex. The parallel coiled coil is generated by a twofold symmetry operation from a 1:1 Rab11–FIP2 complex in the asymmetric unit. Therefore, the two α-helices in the complex are identical. The Rab11–FIP2 ribbons are displayed with transparency. (c) Superposition of the α-helices of FIP2. Identical segments of FIP2 were aligned by a secondary-structure matching algorithm using Coot. The 39 core residues in the α-helices aligned with a root-mean-square (r.m.s.) deviation of 1.8 A for their Cα atoms. |
![[Figure 3]](ft5109fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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