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![[Figure 1]](jb5052fig1mag.jpg)
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Figure 1
Crystal structure of the VcDnaB·VcDciA·ADP:Mg2+ complex. (a) Domain-swapped heterooctamer. The crystal structure of the VcDnaB2·VcDciA2 complex revealed domain swapping between symmetry-related molecules of VcDciA. Left: schematic representation of domain swapping. The NTD and CTD of the two VcDciAs, connected by an extended hinge region (dark blue lines), are exchanged between neighboring molecules related by a true crystallographic twofold rotation axis (red dashed line). The four molecules of VcDnaB are in two shades of blue and green and the four molecules of VcDciA are in pink, purple, orange and brown. The four protein chains of the symmetry mate are marked with a prime. Right: ribbon representation of the heterooctameric structure using the same color code. (b) Structure of the VcDnaB·VcDciA·ADP:Mg2+ heterotetrameric complex forming the unswapped biological assembly, reconstituted from swapped VcDciA domains. Left: schematic representation. The hinges encompassing residues 99–121 of the two VcDciAs are putative in this model (dark blue dotted lines). Right: ribbon representation of the heterotetrameric structure. The VcDnaB dimer is in the same colors as in (a); the two VcDciA molecules are in magenta and yellow. The dark blue dotted rectangle frames the enlarged view shown in (c). (c) Enlargement of the interface region forming a five-helix bundle, with the superimposed experimental electron-density map from SAD phasing after solvent flattening (gray mesh, contoured at 1σ). |
![[Figure 1]](jb5052fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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