 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 2]](ad5015fig2mag.jpg)
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Figure 2
(a) The overall fold of one catalase subunit. β-Strands are shown in blue, α-helices in red, 310-helices in magenta and the haem group and the proximal ligand Tyr337 in green. The N- and C-termini, along with the positions of Arg51 (beginning of the β-barrel), Pro301 (beginning of the wrapping region) and His416 (beginning of the C-terminal region), are indicated. The Leu330–His343 helix with the proximal Fe ligand Tyr337 is seen below the haem group. (b) The catalase tetramer. The suggested entry sites (Fita & Rossmann, 1985  ; Gouet et al., 1995) for subunit A are indicated. The orientations of the P and R axes are shown; the Q axis is perpendicular to the plane of the paper. Note how the N-termini of subunits A (shown from the same orientation as in a) and B penetrate into the wrapping regions of subunits C and D, to the left. |
![[Figure 2]](ad5015fig2.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
