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![[Figure 7]](rr5250fig7mag.jpg)
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Figure 7
Substrate binding in family GH191 and GH114 enzymes. (a) Observed loop conformation of the 120-loop (TmGH191 notation) in the different homologues. An open and closed conformation is observed. In FsGH114 the prominent tip-residue tryptophan is replaced by two tyrosines. (b) Location of a glycerol in TmGH191 (PDB entry 2aam) in subsite −1 and GalN in subsite −2 of AfGH114 (Ega3; PDB entry 6ojb). (c) Observed unexplained density in TmGH191 located between subsite −2 and putative subsite −3. (d) Difference in conformation of the loop between TmGH191 and AfGH114 (Ega3) around Asp64 (TmGH191 notation) that partially closes the active crevice beyond subsite −3 in the bacterial members. |
![[Figure 7]](rr5250fig7.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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