Flavodoxin fold

3chy flavodoxin fold

Flavodoxin Fold

The Flavodoxin Fold is a structural motif found in certain proteins that are involved in electron transfer reactions. Proteins with the Flavodoxin Fold typically contain a characteristic arrangement of secondary structural elements, including a central beta-sheet surrounded by alpha-helices.

Structure

Proteins with the Flavodoxin Fold are characterized by a beta-alpha-beta sandwich structure. This structural motif consists of a central beta-sheet, usually composed of four antiparallel beta-strands, surrounded by alpha-helices on both sides. The beta-sheet serves as a platform for binding cofactors or ligands involved in electron transfer processes.

Function

The Flavodoxin Fold is commonly found in proteins that function as electron carriers or redox enzymes. These proteins play essential roles in various biological processes, such as photosynthesis, respiration, and metabolism. The structural arrangement of the Flavodoxin Fold allows these proteins to efficiently transfer electrons between different molecules or cellular components.

Examples

One well-known example of a protein with the Flavodoxin Fold is flavodoxin, a small electron carrier protein that contains a flavin mononucleotide (FMN) cofactor. Flavodoxins are found in bacteria, archaea, and some eukaryotic organisms, where they participate in electron transfer pathways. Another example is ferredoxin, a protein that contains iron-sulfur clusters and is involved in electron transfer reactions in various metabolic pathways.

Evolutionary Conservation

The Flavodoxin Fold is evolutionarily conserved across different organisms, indicating its importance in biological electron transfer processes. The structural features of the Flavodoxin Fold have been preserved throughout evolution, highlighting its functional significance in maintaining redox balance and energy metabolism.

See also

• Flavodoxin
• Ferredoxin
• Electron transfer
• Protein structure

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