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Alpha/Beta Doubly-Wound Folds
The doubly wound alpha/beta topology was described on the previous page. Some variations of the classic doubly wound fold are illustrated here. In the topology diagrams below, the parts of the chain linking the beta-strands are red, and are thick when they include an alpha-helix. In the RasMol scripts, non-alpha-helical linking regions are shown in pink. Some of the scripts highlight in blue where the fold begins.
flavodoxin,
1flv (127Kb) [Bbk|BNL|ExP|Waw|Hal]
... SCRIPT
subtilisin,
1sbt (172Kb) [Bbk|BNL|ExP|Waw|Hal]
... SCRIPT
arabinose-binding
protein, domain 1,
5abp (217Kb) [Bbk|BNL|ExP|Waw|Hal]
... SCRIPT
glyceraldehyde
phosphate dehydrogenase,
3gpd (443Kb)
[Bbk|BNL|ExP|Waw|Hal]
... SCRIPT
dihydrofolate
reductase, 3dfr (157Kb) [Bbk|BNL|ExP|Waw|Hal]
adenylate
kinase, 3adk (135Kb) [Bbk|BNL|ExP|Waw|Hal]
rhodanese
domain 1, 1rhd (202Kb) [Bbk|BNL|ExP|Waw|Hal]
glutathione
reductase, 1gra (366Kb) [Bbk|BNL|ExP|Waw|Hal]
carboxypeptidase,
2ctb (Kb) [Bbk|BNL|ExP|Waw|Hal]
This fold varies considerably from a classic doubly-wound variation in
order to achieve the arrangement of sheet (mixed parallel and antiparallel
in this case).
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Last updated 7th April '97