Circular permutation in proteins: Difference between revisions

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Circular permutation is a process during

Concanavalin A (left), from PDB: 3cna, and Peanut Lectin (right), from PDB: 2pel, which is homologous to Favin. The termini of the proteins are highlighted by blue and green spheres, and the sequence of residues is indicated by the gradient from blue (N-terminus) to green (C-terminus). The 3-dimensional fold of the two proteins is highly similar, however the N and C- termini are located on different positions of the protein.^[1]

Evolution

A model that can explain how circular permutations can occur during evolution is gene duplication of a precursor gene.^[2] If both genes become fused this leads to a tandem protein. The 5' and 3’ part of the gene can get lost again for example by insertion of a stop codon.

Many

C-termini in close proximity in space.^[3] This characteristic contributes that such permutation events can get tolerated. The amino and carboxy termini of the protein are being fused and different termini introduced, while keeping the overall arrangement of secondary structure elements

essentially unmodified.

Role in protein engineering

Artificially constructed circularly permuted proteins are being used in

biocatalysts and biosensors. For a review on this see.^[3]

References

PMID 16592676. {{cite journal}}: Explicit use of et al. in: |author= (help
)

PMID 10368444
.

^
PMID 21087800
.

PMID 19622546. {{cite journal}}: Explicit use of et al. in: |author= (help
)

PMID 10500161.{{cite journal}}: CS1 maint: multiple names: authors list (link
)

Further reading

David Goodsell (2010) Concanavalin A and Circular Permutation RCSB PDB Molecule of the Month [1]

Retrieved from "https://en.wikipedia.org/w/index.php?title=Circular_permutation_in_proteins&oldid=475902965"

[Cunningham-1] PMID 16592676. {{cite journal}}: Explicit use of et al. in: |author= (help
)

[Jeltsch-2] PMID 10368444
.

[Yu-3] 
PMID 21087800
.

[whitehead-4] PMID 19622546. {{cite journal}}: Explicit use of et al. in: |author= (help
)

[Baird-5] PMID 10500161.{{cite journal}}: CS1 maint: multiple names: authors list (link
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 '''Circular permutation''' is a process during [[evolution]] that changes the order of [[amino acids]] in a [[protein sequence]], resulting in a [[protein structure]] with different connectivity, but overall similar three dimensional shape. As a consequence of the circular permutation, the [[N terminus|N-terminus]] of one [[protein]] shows significant [[sequence similarity]] to the [[C terminus|C-terminus]] of the other and vice versa. Artificially created permutations have been used for various purposes in [[protein engineering]] and [[Protein design|design]]. One of the first naturally occurring circular permutations identified was the swaposin family which are circularly permuted versions of saposins.{{PMID|7610480}}
-[[Image:Concanavalin A vs Lectin.png|thumb|Two proteins that are related by a circular permutation: [[Concanavalin a|Concanavalin A]] (left) {{PDB|3cna}}, and Peanut Lectin (right), {{PDB|2pel}}. The two proteins are colored using a “rainbow” coloring scheme, showing the N-terminus in red and C-terminus in blue. As can be seen, the 3-dimensional fold is highly similar; however, the N and C- termini are located on different positions of the protein.<ref name="Cunningham">{{cite journal |author=Cunningham et al |year=1976 |title=Favin versus concanavalin A: Circularly permuted amino acid sequences |journal=PNAS |volume= 76|issue=7 |pages=3218–3222 |pmid=16592676 |doi=10.1073/pnas.76.7.3218 |pmc=383795}}</ref>]]
+[[Image:Concanavalin A vs Lectin.png|thumb| Two proteins that are related by a circular permutation: [[Concanavalin_a|Concanavalin A]] (left), from {{PDB|3cna}}, and Peanut Lectin (right), from {{PDB|2pel}}, which is homologous to Favin. The termini of the proteins are highlighted by blue and green spheres, and the sequence of residues is indicated by the gradient from blue (N-terminus) to green (C-terminus). The 3-dimensional fold of the two proteins is highly similar, however the N and C- termini are located on different positions of the protein.<ref name="Cunningham">{{cite journal |author=Cunningham et al |year=1976 |title=Favin versus concanavalin A: Circularly permuted amino acid sequences |journal=PNAS |volume= 76|issue=7 |pages=3218–3222 |pmid=16592676 |doi=10.1073/pnas.76.7.3218 |pmc=383795}}</ref>]]
 ==Evolution==