The 1.5 Å structure of endo-1,3-β-glucanase from Streptomyces sioyaensis: Evolution of the active-site structure for 1,3-β-glucan-binding specificity and hydrolysis

Tang Yao Hong, Yu-Yuan Hsiao, Menghsiao Meng, Tien Hsiung Thomas Li

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

The catalytic domain structure of Streptomyces sioyaensis 1,3-β-glucanase (278 amino acids), a member of glycosyl hydrolase family 16 (GHF16), was determined to 1.5 Å resolution in space group P212121. The enzyme specifically hydrolyzes the glycosidic bond of the 1,3-β-linked glucan substrate. The overall structure contains two antiparallel six-and seven-stranded β-sheets stacked in a β-sandwich jelly-roll motif similar to the fold of GHF16 1,3-1,4-β-glucanases. The active-site cleft of the enzyme is distinct, with the closure of one end primarily caused by two protruding loop insertions and two key residues, Tyr38 and Tyr134. The current known structures of 1,3-1,4-β-glucanases and 1,3-β-glucanase from Nocardiopsis sp., on the other hand, have open-channel active-site clefts that can accommodate six β-d-glucopyranosyl units. The active-site structure of 1,3-β-glucanase was compared with those of other homologous structures in order to address the binding and enzymatic specificity for 1,3-β-linked glucans in Streptomyces. This information could be helpful in the development of specific antifungal agents.

Original languageEnglish
Pages (from-to)964-970
Number of pages7
JournalActa Crystallographica Section D: Biological Crystallography
Volume64
Issue number9
DOIs
StatePublished - 13 Aug 2008

Keywords

  • Endo-1,3-β-glucanases
  • Glycosyl hydrolases

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