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Structure paper

TitlePgaB orthologues contain a glycoside hydrolase domain that cleaves deacetylated poly-beta (1,6)-N-acetylglucosamine and can disrupt bacterial biofilms.
Journal, issue, pagesPLoS Pathog., Vol. 14, Page e1006998-e1006998, Year 2018
Publish dateAug 30, 2017 (structure data deposition date)
AuthorsLittle, D.J. / Pfoh, R. / Le Mauff, F. / Bamford, N.C. / Notte, C. / Baker, P. / Guragain, M. / Robinson, H. / Pier, G.B. / Nitz, M. ...Little, D.J. / Pfoh, R. / Le Mauff, F. / Bamford, N.C. / Notte, C. / Baker, P. / Guragain, M. / Robinson, H. / Pier, G.B. / Nitz, M. / Deora, R. / Sheppard, D.C. / Howell, P.L.
External linksPLoS Pathog. / PubMed:29684093
MethodsX-ray diffraction
Resolution1.76 Å
Structure data

PDB-6au1:
Structure of the PgaB (BpsB) glycoside hydrolase domain from Bordetella bronchiseptica
Method: X-RAY DIFFRACTION / Resolution: 1.76 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • bordetella bronchiseptica (bacteria)
KeywordsHYDROLASE / deacetylase / glycoside hydrolase / PNAG / biofilm

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