 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](ji5030fig1mag.jpg)
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Figure 1
Comparison of Colchicalin in the presence or absence of the ligand colchicine. (a) Amino-acid sequence alignment of Colchicalin D6.2, crystallized in this study without ligand, with the previously crystallized Colchicalin Δ4-D6.3 in complex with colchicine (Barkovskiy et al., 2019  ) as well as wild-type Lcn2. Positions Ile97, Lys98 and Ser99 on loop #3, which do not directly contact the ligand, exhibit the largest deviation between the apo and complexed states of Colchicalin and are marked in blue. (b) Overall architecture of the previously described Colchicalin Δ4-D6.3 in complex with colchicine (orange). (c) Overall architecture of Colchicalin D6.2 in its apo state. The marked conformational rearrangement of loop #3 is evident (loops colored magenta and cyan, respectively). (d) Spatial deviation between Cα positions in the crystal structure of apo Colchicalin versus the Colchicalin–colchicine complex after superposition via the 58 conserved Cα atoms in the lipocalin fold (Skerra, 2000). The structurally variable loop regions 1–4 are indicated. Note the high values for loop #3. (e, f) B-factor plots for the two Colchicalin crystal structures. The average B-factor values are shown separately for the main-chain atoms (solid lines) and side-chain atoms (broken lines) of each residue in the apoprotein (e) and the Colchicalin–colchicine complex (f). |
![[Figure 1]](ji5030fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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