 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](kw5005fig2mag.jpg)
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Figure 2
(a) Ribbon diagram of the structure of one MnSOD-3 subunit (PDB code 3dc5 ). The N- and C-domains are shown in light and dark blue, respectively, with the N- and C-termini indicated. Although the N-terminal domain appears to consist of two long helices, each of these is disrupted by a single additional residue (positions 29 and 60, respectively) that bulges out, with the main-chain carbonyl excluded from the regular hydrogen-bonding pattern. The first long helix is therefore comprised of two turns of α1 followed by six turns of α2, while the second has two turns of α3 followed by five turns of α4. α2 and α3 are linked by a hairpin and form a four-helix bundle at the tetramer interface. (b) Ribbon diagram of the MnSOD-3 tetramer colored by subunit. The blue subunit is in the same orientation shown in (a). The two four-helix bundles of the tetramer interface can be clearly seen centered in the figure. The manganese and hydroxyl ions are also shown in magenta and red, respectively. This figure was produced using PyMOL (DeLano, 2008  ) |
![[Figure 2]](kw5005fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
