Flavodoxin fold

Ribbon diagram of CheY (a regulator of the chemotactic response in bacteria, PDB accession code 3CHY), which adopts the flavodoxin fold. Ribbon is colored from blue (N-terminus) to red (C-terminus).

The flavodoxin fold is a common α/β protein fold, second only to the TIM barrel fold. It has three layers, with two α-helical layers sandwiching a 5-stranded parallel β-sheet. The order of strands within the sheet is 2-1-3-4-5.

This motif is present for example in lactate dehydrogenase (PDB: 1A5Z​) or phosphoglycerate kinase (PDB: 1FW8​).[1]

External links

  • SCOP list of proteins adopting the flavodoxin fold Archived 2018-12-07 at the Wayback Machine (mirror)

References

  1. ^ Kalinowska B, Banach M, Wiśniowski Z, Konieczny L, Roterman I (July 2017). "Is the hydrophobic core a universal structural element in proteins?". Journal of Molecular Modeling. 23 (7): 205. doi:10.1007/s00894-017-3367-z. PMC 5487895. PMID 28623601.
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Protein tertiary structure
General
  • Structural domain
  • Protein folding
  • Structure determination methods
All-α folds:
  • Helix bundle
  • Globin fold
  • Homeodomain fold
  • Alpha solenoid
  • Death fold
All-β folds:
  • Immunoglobulin domain
  • Beta barrel
  • Beta-propeller
  • Beta helix
α/β folds:
α+β folds:
Irregular folds: