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Structure paper

TitleAlternative folding to a monomer or homopolymer is a common feature of the type 1 pilus subunit FimA from enteroinvasive bacteria.
Journal, issue, pagesJ. Biol. Chem., Year 2019
Publish dateAug 12, 2016 (structure data deposition date)
AuthorsZyla, D.S. / Prota, A.E. / Capitani, G. / Glockshuber, R.
External linksJ. Biol. Chem. / PubMed:31126987
MethodsX-ray diffraction
Resolution0.886266337349 - 1.69 Å
Structure data

PDB-5lp9:
FimA wt from S. flexneri
Method: X-RAY DIFFRACTION / Resolution: 0.886266337349 Å

PDB-5nkt:
FimA wt from E. coli
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-6erj:
Self-complemented FimA subunit from Salmonella enterica
Method: X-RAY DIFFRACTION / Resolution: 1.69 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-ACY:
ACETIC ACID

Source
  • shigella flexneri (bacteria)
  • escherichia coli k-12 (bacteria)
  • salmonella paratyphi a (strain atcc 9150 / sarb42) (bacteria)
KeywordsSTRUCTURAL PROTEIN / FimA / pilus / monomer / subunit / pili / Shigella / flexneri / pathogenic / main structural subunit / high resolution / Escherichia / coli / tyle-1 pilus / type-1 pili / salmonella / enterica / immunoglobulin-like / fold / self-complemented

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