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TitleA Bacteroidetes locus dedicated to fungal 1,6-beta-glucan degradation: Unique substrate conformation drives specificity of the key endo-1,6-beta-glucanase.
Journal, issue, pagesJ. Biol. Chem., Vol. 292, Page 10639-10650, Year 2017
Publish dateMar 17, 2017 (structure data deposition date)
AuthorsTemple, M.J. / Cuskin, F. / Basle, A. / Hickey, N. / Speciale, G. / Williams, S.J. / Gilbert, H.J. / Lowe, E.C.
External linksJ. Biol. Chem. / PubMed:28461332
MethodsX-ray diffraction
Resolution1.85 - 1.9 Å
Structure data

PDB-5ngk:
The endo-beta1,6-glucanase BT3312
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-5ngl:
The endo-beta1,6-glucanase BT3312
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

Source
  • bacteroides thetaiotaomicron (bacteria)
KeywordsHYDROLASE / glycoside hydrolase / endo-beta1 / 6-clucanase / beta-1 / 6-glucan / Bacteroides / human gut microbiota / yeast glycan / glycoside hydrolase; endo-beta1 / 6-clucanase; beta-1 / 6-glucan; Bacteroides; human gut microbiota; yeast glycan

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