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Structure paper

TitleStructural and biochemical characterization of a multidomain alginate lyase reveals a novel role of CBM32 in CAZymes
Journal, issue, pagesBiochim. Biophys. Acta, Vol. 1862, Page 1862-1869, Year 2018
Publish dateMay 7, 2018 (structure data deposition date)
AuthorsLyu, Q. / Zhang, K. / Zhu, Q. / Li, Z. / Liu, Y. / Fitzek, E. / Yohe, T. / Zhao, L. / Li, W. / Liu, T. ...Lyu, Q. / Zhang, K. / Zhu, Q. / Li, Z. / Liu, Y. / Fitzek, E. / Yohe, T. / Zhao, L. / Li, W. / Liu, T. / Yin, Y. / Liu, W.
External linksBiochim. Biophys. Acta / PubMed:29864445
MethodsX-ray diffraction
Resolution1.4 - 1.6 Å
Structure data

PDB-5zu5:
Crystal structure of a full length alginate lyase with CBM domain
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-5zu6:
A CBM32 derived from alginate lyase B (AlyB-OU02)
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • vibrio splendidus (bacteria)
  • vibrio (bacteria)
KeywordsLYASE / alginate lyase / PL7 / CBM / CBM32

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