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Structure paper

TitleGroup AStreptococcusT Antigens Have a Highly Conserved Structure Concealed under a Heterogeneous Surface That Has Implications for Vaccine Design.
Journal, issue, pagesInfect. Immun., Vol. 87, Year 2019
Publish dateOct 19, 2017 (structure data deposition date)
AuthorsYoung, P.G. / Raynes, J.M. / Loh, J.M. / Proft, T. / Baker, E.N. / Moreland, N.J.
External linksInfect. Immun. / PubMed:30936156
MethodsX-ray diffraction
Resolution1.75 - 1.9 Å
Structure data

PDB-6bbt:
Structure of the major pilin protein (T-13) from Streptococcus pyogenes serotype GAS131465
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-6bbw:
Structure of the major pilin protein (T3.2) from Streptococcus pyogenes serotype GAS13637
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-6n0a:
Structure of the major pilin protein (T-18.1) from Streptococcus pyogenes serotype MGAS8232
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-CA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • streptococcus pyogenes (bacteria)
KeywordsSTRUCTURAL PROTEIN / Trypsin-resistant surface protein Tee13 / Lancefield T-antigen / Serotyping / Pili / Fimbriae Proteins / Streptococcus pyogenes / isopeptide bond. / Trypsin-resistant surface protein T3.2 / Major pilin backbone protein / T-antigen / T18.1

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