Ferredoxin fold

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2acy ferredoxin fold

Ferredoxin Fold

The Ferredoxin Fold is a structural motif found in proteins that are involved in electron transfer reactions. Proteins with the Ferredoxin Fold typically contain iron-sulfur clusters that serve as electron carriers. The fold is named after ferredoxins, which were the first proteins discovered to have this characteristic structure.

Structure

Proteins with the Ferredoxin Fold are characterized by a beta-alpha-beta secondary structure motif. This motif consists of a beta sheet sandwiched between alpha helices. The beta sheet is typically composed of four anti-parallel beta strands, with the alpha helices located on either side.

Function

The Ferredoxin Fold is commonly found in proteins that participate in redox reactions, where electrons are transferred between molecules. These proteins often play crucial roles in metabolic pathways, photosynthesis, and other biological processes that involve electron transport chains.

Examples

One of the most well-known proteins with the Ferredoxin Fold is ferredoxin itself, a small iron-sulfur protein that functions as an electron carrier in various metabolic pathways. Other proteins that contain the Ferredoxin Fold include flavodoxins, which are flavin-containing electron carriers, and certain enzymes involved in oxidative phosphorylation.

Significance

The presence of the Ferredoxin Fold in a protein can provide valuable insights into its function and evolutionary history. By studying the structure and function of proteins with this motif, researchers can gain a better understanding of how organisms utilize electron transfer processes to carry out essential biological functions.

See also

• Ferredoxin
• Flavodoxin
• Iron-sulfur cluster