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Structure paper

TitleThe molecular basis of endolytic activity of a multidomain alginate lyase fromDefluviitalea phaphyphila, a representative of a new lyase family, PL39.
Journal, issue, pagesJ. Biol. Chem., Vol. 294, Page 18077-18091, Year 2019
Publish dateMar 25, 2019 (structure data deposition date)
AuthorsJi, S. / Dix, S.R. / Aziz, A.A. / Sedelnikova, S.E. / Baker, P.J. / Rafferty, J.B. / Bullough, P.A. / Tzokov, S.B. / Agirre, J. / Li, F.L. / Rice, D.W.
External linksJ. Biol. Chem. / PubMed:31624143
MethodsX-ray diffraction
Resolution2.069 - 2.85 Å
Structure data

PDB-6jp4:
Crystal structure of the catalytic domain of a multi-domain alginate lyase Dp0100 from thermophilic bacterium Defluviitalea phaphyphila
Method: X-RAY DIFFRACTION / Resolution: 2.069 Å

PDB-6jph:
Crystal structure of the catalytic domain of a multi-domain alginate lyase Dp0100 from thermophilic bacterium Defluviitalea phaphyphila
Method: X-RAY DIFFRACTION / Resolution: 2.759 Å

PDB-6jpn:
Crystal structure of the catalytic domain of a multi-domain alginate lyase Dp0100 from thermophilic bacterium Defluviitalea phaphyphila
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CAC:
CACODYLATE ION

ChemComp-HOH:
WATER

Source
  • defluviitalea phaphyphila (bacteria)
KeywordsLYASE / alpha barrel+beta sandwich

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