Ferredoxin fold

Ribbon diagram of acylphosphatase (PDB accession code 2ACY), which adopts a ferredoxin fold with an extra β-strand at the C-terminus (shown in red). The ribbon is colored from blue (N-terminus) to red (C-terminus).

In protein structure, a ferredoxin fold is a common α+β protein fold with a signature βαββαβ secondary structure along its backbone. Structurally, the ferredoxin fold can be regarded as a long, symmetric hairpin that is wrapped once around, so that its two terminal β-strands hydrogen-bond to the central two β-strands, forming a four-stranded, antiparallel β-sheet covered on one side by two α-helices.

External links

  • SCOP list of proteins with a ferredoxin-like fold

References

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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:


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