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Structure paper

TitlePorphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide.
Journal, issue, pagesCommun Biol, Vol. 4, Page 106-106, Year 2021
Publish dateDec 8, 2019 (structure data deposition date)
AuthorsHeidler, T.V. / Ernits, K. / Ziolkowska, A. / Claesson, R. / Persson, K.
External linksCommun Biol / PubMed:33495563
MethodsX-ray diffraction
Resolution1.8 - 1.85 Å
Structure data

PDB-6tnj:
Crystal structure of the vWF domain of the type V pili tip protein Mfa5 from Porphyromonas gingivalis
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-6to1:
Crystal structure of three N-terminal domains of the type V pili tip protein Mfa5 from Porphyromonas gingivalis
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-MPO:
3[N-MORPHOLINO]PROPANE SULFONIC ACID / pH buffer*YM

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

Source
  • porphyromonas gingivalis atcc 33277 (bacteria)
KeywordsCELL ADHESION / Intramolekular Isopeptide / von Willebrand factor / Bacterial adhesion / Phorphyromonas gingivalis / Mfa1 fimbriae / Type V pili / P. gingivalis

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