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Structure paper

TitleAn internal thioester in a pathogen surface protein mediates covalent host binding.
Journal, issue, pagesElife, Vol. 4, Year 2015
Publish dateApr 17, 2015 (structure data deposition date)
AuthorsWalden, M. / Edwards, J.M. / Dziewulska, A.M. / Bergmann, R. / Saalbach, G. / Kan, S.Y. / Miller, O.K. / Weckener, M. / Jackson, R.J. / Shirran, S.L. ...Walden, M. / Edwards, J.M. / Dziewulska, A.M. / Bergmann, R. / Saalbach, G. / Kan, S.Y. / Miller, O.K. / Weckener, M. / Jackson, R.J. / Shirran, S.L. / Botting, C.H. / Florence, G.J. / Rohde, M. / Banfield, M.J. / Schwarz-Linek, U.
External linksElife / PubMed:26032562
MethodsX-ray diffraction
Resolution1.3 - 2.62 Å
Structure data

PDB-5a0d:
N-terminal thioester domain of surface protein from Clostridium perfringens, Cys138Ala mutant
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-5a0g:
N-terminal thioester domain of surface protein from Clostridium perfringens
Method: X-RAY DIFFRACTION / Resolution: 2.62 Å

PDB-5a0l:
N-terminal thioester domain of fibronectin-binding protein SfbI from Streptococcus pyogenes
Method: X-RAY DIFFRACTION / Resolution: 1.35 Å

PDB-5a0n:
N-terminal thioester domain of protein F2 like fibronectin-binding protein from Streptococcus pneumoniae
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-GOL:
GLYCEROL

Source
  • clostridium perfringens (bacteria)
  • streptococcus pyogenes (bacteria)
  • streptococcus pneumoniae (bacteria)
KeywordsCELL ADHESION / SURFACE-ASSOCIATED PROTEIN / GRAM-POSITIVE / ADHESIN / INTERNAL THIOESTER / THIOESTER DOMAIN

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