Structure-guided analysis of catalytic specificity of the abundantly secreted chitosanase SACTE_5457 from Streptomyces sp. SirexAA-E.

@article{Takasuka2014StructureguidedAO,
  title={Structure-guided analysis of catalytic specificity of the abundantly secreted chitosanase SACTE_5457 from Streptomyces sp. SirexAA-E.},
  author={Taichi E. Takasuka and Christopher M. Bianchetti and Yuki Tobimatsu and Lai F. Bergeman and John Ralph and Brian G. Fox},
  journal={Proteins},
  year={2014},
  volume={82 7},
  pages={1245-57}
}
SACTE_5457 is secreted by Streptomyces sp. SirexAA-E, a highly cellulolytic actinobacterium isolated from a symbiotic community composed of insects, fungi, and bacteria. Here we report the 1.84 Å resolution crystal structure and functional characterization of SACTE_5457. This enzyme is a member of the glycosyl hydrolase family 46 and is composed of two α-helical domains that are connected by an α-helical linker. The catalytic residues (Glu74 and Asp92) are separated by 10.3 Å, matching the… CONTINUE READING
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