 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](nw5110fig1mag.jpg)
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Figure 1
Active-site motifs of CE4 enzymes. The general base and acid catalyst residues are highlighted in green and cyan, respectively. The metal-binding triad is highlighted in yellow. Percent identity indicates the homology of the region corresponding to the catalytic domain of TTE0866 (residues 136–324). The letters correspond to Supplementary Fig. S6. (a) BsPdaC (Bacillus subtilis subsp. subtilis; Grifoll-Romero et al., 2019  ), (b) ArCE4 (Arthrobacter sp.; Tuveng et al., 2017), (c) SlAXE (Streptomyces lividans; Taylor et al., 2006), (d) Xyl-CE4 (uncultured bacterium), (e) BA3943 (B. anthracis), (f) BcPdgA (BC1960; B. cereus; Fadouloglou et al., 2017), (g) SpPgdA (Streptococcus pneumoniae; Blair et al., 2005), (h) BC1974 (B. cereus; Giastas et al., 2018), (i) CtAXE (Acetivibrio thermocellus; Taylor et al., 2006), (j) BA0150 (B. anthracis; Strunk et al., 2014), (k) BaCE4 (BA0424) (B. anthracis; Oberbarnscheidt et al., 2007), (l) ClCDA (Colletotrichum lindemuthianum; Blair et al., 2006), (m) SmPgdA (S. mutans; Deng et al., 2009), (n) Bd3279 (Bdellovibrio bacteriovorus; Lambert et al., 2016), (o) BsPgaA (B. subtilis; Blair & van Aalten, 2004) and (p) AnCDA (Aspergillus nidulans; Liu et al., 2017). |
![[Figure 1]](nw5110fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
