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![[Figure 4]](cb5130fig4mag.jpg)
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Figure 4
Images of Hjc_15-6 as a tetramer. Chains A and B in dimer I are shown as dark and light blue ribbons and chains A and B in dimer II are shown as dark red and pink ribbons in (a), (b), (d), (f) and (h). The active-site residues Glu10, Asp40, Glu53 and Lys55 are drawn as cylinders and coloured according to atom type in (b), (d) and (g). Phosphate/sulfate groups are drawn as sulfate groups with cylinders coloured according to atom type in (b), (c), (e), (f) and (g). In (e) the electrostatic surface potential is transparent, with bloboids of active-site residues coloured in green (dimer I) and pink (dimer II). In (a) it can be seen that dimer I is in front of dimer II. In (b)–(e) all images are displayed at the same angle, revealing a tunnel in the centre of the Hjc_15-6 tetramer that is viewed as a close-up in (d), where two distances have been measured. (f) and (g) present views rotated from the bottom to the top by 90° from those in (b)–(e), revealing a cleft between chain A in dimer I and chain B in dimer II. In (h) and (i) the tetramer is further rotated 90° to the left compared with (f) and (g), revealing another cleft between chain A in dimer II and chain B in dimer I. |
![[Figure 4]](cb5130fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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