 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](dz5280fig1mag.jpg)
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Figure 1
Overall structure and proteolytic chamber of MtaLonC. (a) Domain organization in the primary structures of the MtaLonC, LonA and LonB proteases. The N-terminal coil of MtaLonC is coloured red. (b) The MtaLonC monomer as a tube diagram, with similar colouring as in (a), superimposed with TonLonB (PDB entry 3k1j , chain A; grey). The substrate-binding groove between the β1–β2 hairpin (green) and the β4–α3 loop (yellow) is indicated by the arrowhead. (c) View of the top axial pore (13 Å in diameter) of MtaLonC in ribbon representation with a semi-transparent surface (left); domains are coloured as in (b). Dashed lines represent the directions of the cutting planes to produce the views in (d) and (e). A cutaway top view is shown on the right, revealing the six proteolytic sites and the bottom axial opening (15 Å in diameter) formed by six protease domains. The catalytic dyad, noncatalytic Asp581, β1–β2 hairpin and β4–α3 loop (see text) are coloured red, magenta, green and yellow, respectively. (d, e) Two cutaway side views of the proteolytic chamber. Open arrowheads indicate openings to the surface; black arrowheads mark the substrate-binding grooves. |
![[Figure 1]](dz5280fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
