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Structure paper

TitleDonor strand sequence, rather than donor strand orientation, determines the stability and non-equilibrium folding of the type 1 pilus subunit FimA.
Journal, issue, pagesJ. Biol. Chem., Vol. 295, Page 12437-12448, Year 2020
Publish dateMar 28, 2019 (structure data deposition date)
AuthorsZyla, D. / Echeverria, B. / Glockshuber, R.
External linksJ. Biol. Chem. / PubMed:32651228
MethodsX-ray diffraction
Resolution1.502 - 1.81 Å
Structure data

PDB-6r74:
N-terminally reversed variant of FimA E. coli
Method: X-RAY DIFFRACTION / Resolution: 1.81 Å

PDB-6r7e:
N-terminally reversed variant of FimA E. coli with alanine insertion at position 20
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

PDB-6s09:
C-terminally extended and N-terminally truncated variant of FimA E. coli at 1.5 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 1.502 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-NA:
Unknown entry

ChemComp-ACY:
ACETIC ACID

Source
  • escherichia coli (E. coli)
KeywordsSTRUCTURAL PROTEIN / FimA / pilus / monomer / subunit / pili / synthetic / construct / main structural subunit / high resolution / N terminus / reversed / C terminus / Oligo Glycine / Linker

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