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).
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. Diagram of Î’-Pleated sheet and bond structure of protein The β sheet (also β-pleated sheet) is a commonly occurring form of regular secondary structure in proteins, first proposed by Linus Pauling and Robert Corey in 1951. ... Diagram of Î’-Pleated sheet and bond structure of protein The β sheet (also β-pleated sheet) is a commonly occurring form of regular secondary structure in proteins, first proposed by Linus Pauling and Robert Corey in 1951. ... Diagram of Î’-Pleated sheet and bond structure of protein The β sheet (also β-pleated sheet) is a commonly occurring form of regular secondary structure in proteins, first proposed by Linus Pauling and Robert Corey in 1951. ...
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