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![[Figure 5]](jc5051fig5mag.jpg)
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Figure 5
The role of the GbpA2 domain in crystal packing. (a) The GbpA2 domain in the CbpD structure (yellow cylinder) is displaced by 1 Å and rotated by 135.6° relative to the GbpA2 domain in the GbpA structure (light blue cylinder) when their AA10 domains are aligned. The αG of each GbpA2 domain (smaller cylinders), the β12–β13 hairpins (stylized cartoons) and the C-termini are indicated for orientation. The AA10 domain of CbpD is represented as in Fig. 2 ![[link]](../../../../../../logos/arrows/d_arr.gif) (a), with copper modeled into the active site as a sphere (sphere_scale 0.6). The displacement of GbpA2 domains is also noted by the ND2 label at the shifted N-terminus of this domain in GbpA. (b) β15 and part of the linker between the GbpA2 and CBM73 domains of one CbpD (yellow and dark gray) engage in extensive β-strand interactions with a symmetry mate (orange and light gray) to form an extended β-sheet, burying 990 Å2 of surface area per monomer. |
![[Figure 5]](jc5051fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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