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Protein folds propelled by diversity.
1Department of Biochemistry, University of Cambridge, Tennis Court Road, CB2 1QW, Cambridge, UK. max@cryst.bioc.cam.ac.uk
Progress in Biophysics and Molecular Biology
|June 8, 2001
Summary
Beta-propeller proteins are modular and diverse, folding via beta-sheets. Despite sequence variation, conserved structural features like hydrogen bonds and hydrophobic contacts stabilize this protein fold.
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- Proteins are crucial for biological processes and often exhibit modular structures.
- Beta-propeller proteins are a diverse group that fold by arranging four-stranded beta-sheets circularly.
Purpose of the Study:
- To review the structural features of beta-propeller proteins.
- To identify conserved elements and stabilizing interactions within this protein fold.
- To explore methods for detecting novel beta-propeller proteins.
Main Methods:
- Comparison of available structural coordinates of beta-propeller proteins.
- Structure-based sequence alignments.
- Analysis of superpositions of individual modular units.
Main Results:
- Conserved features include hydrogen bonds, beta-turns, and hydrophobic contacts, despite low sequence identity.
- Specific interactions, like recurring aspartates, stabilize the fold.
- The size of hydrophobic residues dictates the number of beta-sheets in the array.
Conclusions:
- The beta-propeller fold is stabilized by conserved structural interactions rather than sequence homology.
- New members of this fold can potentially be identified using sequence searches that consider modular assembly and key residue positions.