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Structure paper

TitleUnravelling the specificity and mechanism of sialic acid recognition by the gut symbiont Ruminococcus gnavus.
Journal, issue, pagesNat Commun, Vol. 8, Page 2196-2196, Year 2017
Publish dateOct 16, 2017 (structure data deposition date)
AuthorsOwen, C.D. / Tailford, L.E. / Monaco, S. / Suligoj, T. / Vaux, L. / Lallement, R. / Khedri, Z. / Yu, H. / Lecointe, K. / Walshaw, J. ...Owen, C.D. / Tailford, L.E. / Monaco, S. / Suligoj, T. / Vaux, L. / Lallement, R. / Khedri, Z. / Yu, H. / Lecointe, K. / Walshaw, J. / Tribolo, S. / Horrex, M. / Bell, A. / Chen, X. / Taylor, G.L. / Varki, A. / Angulo, J. / Juge, N.
External linksNat Commun / PubMed:29259165
MethodsX-ray diffraction
Resolution1.3 - 1.73 Å
Structure data

PDB-6er2:
Ruminococcus gnavus IT-sialidase CBM40
Method: X-RAY DIFFRACTION / Resolution: 1.73 Å

PDB-6er3:
Ruminococcus gnavus IT-sialidase CBM40 bound to alpha2,3 sialyllactose
Method: X-RAY DIFFRACTION / Resolution: 1.37 Å

PDB-6er4:
Ruminococcus gnavus IT-sialidase CBM40 bound to alpha2,6 sialyllactose
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

Source
  • ruminococcus gnavus atcc 29149 (bacteria)
KeywordsSUGAR BINDING PROTEIN / sialidase / CBM / sialic acid

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