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Proteopedia: Rossmann fold: A beta-alpha-beta fold at dinucleotide binding sites
1Faculty of Natural Sciences, Ariel University, Ariel, 40700, Israel.
Summary
The Rossmann fold, a common protein structure, features a conserved beta-alpha-beta motif crucial for binding dinucleotides like NAD and FAD. This structure facilitates coenzyme binding through specific interactions with the adenosine diphosphate component.
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- The Rossmann fold is a prevalent super-secondary structure in proteins.
- It consists of alternating beta strands (β) and alpha helices (α), forming a β-sheet.
- The core beta-alpha-beta (βαβ) motif is highly conserved and recognized as an 'ADP-binding βαβ fold'.
Purpose of the Study:
- To illustrate the structural characteristics of Rossmann folds.
- To highlight the commonalities in FAD and NAD(P)-binding proteins.
- To explain the role of the βαβ fold in coenzyme binding.
Main Methods:
- Structural analysis of FAD and NAD(P)-binding proteins.
- Comparative study of the Rossmann fold motif.
- Review of existing literature and databases (e.g., Proteopedia).
Main Results:
- FAD and NAD(P) coenzymes share a common adenosine diphosphate (ADP) structure.
- The βαβ fold motif accommodates the ADP component of these coenzymes.
- Specific interactions, including conserved glycines (Gly-x-Gly), facilitate ADP binding within the fold.
Conclusions:
- The Rossmann fold's conserved βαβ motif is essential for binding ADP-containing coenzymes.
- Structural features, like the hairpin turn and conserved glycines, are critical for coenzyme recognition and binding.
- Variations in the structure surrounding the core βαβ motif allow for diverse protein functions.
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