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![[Figure 4]](jb5052fig4mag.jpg)
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Figure 4
DciA binds to the periphery of the DnaB CTD. (a) Structure of the VcDnaB6·VcDciA6 heterododecameric complex reconstituted by the crystal H32 symmetry. The color code is the same as in Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif){kind=small} (b). Left: schematic representation. The heterododecameric ring is reconstituted by assembly of the heterotetramer with two neighboring symmetry mates (hatched textures) related by a true crystallographic threefold rotation axis (red dashed lines). The hinges encompassing residues 99–121 of the VcDciA molecules are putative in this unswapped model (dark blue dotted lines). Right: ribbon representation of the heterododecameric model. (b) Structural comparison of four helicase-loader complexes: VcDnaB·VcDciA (PDB entry 8a3v, this study), EcDnaB·EcDnaC (PDB entry 6qel), EcDnaB·λP (PDB entry 6bbm) and GstDnaB·BsDnaI (extracted from PDB entry 4m4w). The DnaB hexamers are represented as surfaces (blue and green) and the helicase loaders as magenta sticks. Unlike DnaC, λP and DnaI, which cover the back of the DnaB CTD ring, DciA leaves it free by positioning itself at the periphery of the helicase. |
![[Figure 4]](jb5052fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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