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![[Figure 4]](nz5009fig4mag.jpg)
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Figure 4
Activation of astacins with reported zymogen structures and a conserved PP motif. (a)–(d) Superposition in cross-eyed stereo of the Cα traces in standard orientation of the latent and mature forms of (a) Limulus astacin (latent, PDB entry 8a28; mature, AlphaFold model), (b) crayfish astacin [latent, PDB entry 3lq0 (Guevara et al., 2010  ); mature, PDB entry 1ast (Bode et al., 1992; Gomis-Rüth et al., 1993)], (c) human meprin β [latent, PDB entry 4gwm (Arolas et al., 2012); mature, PDB entry 4gwn (Arolas et al., 2012)] and (d) Myroides sp. CSLBB myroilysin [latent, PDB entry 5gwd (Xu et al., 2017); mature, PDB entry 5zjk (Ran et al., 2020)]. The mature forms are in orange and the zymogens are in cyan (PP) and yellow (CD). The catalytic zinc ions are depicted as purple spheres. The PP of meprin β is N-terminally extended and runs across the front surface of a vicinal TRAF domain (not shown; Arolas et al., 2012). The most relevant rearranged segments during maturation cleavage, the `activation segment' and the mature N-terminal segment, are pinpointed by green and red stars in each structure, respectively. (e) Superposition of the segments encompassing the PP motif of astacins (F-E-G-D-I) in pLAST (C atoms in cyan), crayfish pro-astacin (C atoms in tan) and human pro-meprin β (C atoms in plum). Myroilysin lacks this motif. |
![[Figure 4]](nz5009fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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