TY - JOUR
T1 - The 1.5 Å structure of endo-1,3-β-glucanase from Streptomyces sioyaensis
T2 - Evolution of the active-site structure for 1,3-β-glucan-binding specificity and hydrolysis
AU - Hong, Tang Yao
AU - Hsiao, Yu-Yuan
AU - Meng, Menghsiao
AU - Li, Tien Hsiung Thomas
PY - 2008/8/13
Y1 - 2008/8/13
N2 - 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.
AB - 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.
KW - Endo-1,3-β-glucanases
KW - Glycosyl hydrolases
UR - http://www.scopus.com/inward/record.url?scp=49749127692&partnerID=8YFLogxK
U2 - 10.1107/S0907444908021550
DO - 10.1107/S0907444908021550
M3 - Article
C2 - 18703845
AN - SCOPUS:49749127692
VL - 64
SP - 964
EP - 970
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 0907-4449
IS - 9
ER -