 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](pu0032fig1mag.jpg)
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Figure 1
Sf-caspase-1/P35 complex structure. (a) Molecular-replacement solution of the complex between P35 in green and Sf-caspase-1 in blue. A portion of the reactive-site loop of P35 extends towards the active site of the Sf-caspase-1 formed by the p19–p12 subunits. Residue 84 marks the position of the P4 residue entering the active site of Sf-caspase-1. The P35 N-terminus (as seen in the V71P caspase-cleaved mutant) is displayed. (b) The biologically relevant complex viewed down the crystallographic twofold axis. This view is rotated 90° along a vertical axis compared to the orientation in (a). The Sf-caspase-1 functional dimer of heterodimers is generated by crystallographic twofold symmetry operation on one p19–p12 dimer (red) to generate the other dimer (blue). The two P35s in green occupy the two Sf-caspase-1 active sites. |
![[Figure 1]](pu0032fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
