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Structure and characterization of a novel chicken biotin-binding protein A (BBP-A)

Hytönen, Vesa P; Niskanen, Einari A; Huuskonen, Juhani; Määttä, Juha A E (Tay); Nordlund, Henri R (Tay); Kulomaa, Markku S (Tay) (2007)

 
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structure_and_characterization_2007.pdf (2.487Mt)
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Hytönen, Vesa P
Niskanen, Einari A
Huuskonen, Juhani
Määttä, Juha A E (Tay)
Nordlund, Henri R (Tay)
Kulomaa, Markku S (Tay)
2007

BMC Structural Biology 7
8
This publication is copyrighted. You may download, display and print it for Your own personal use. Commercial use is prohibited.
doi:10.1186/1472-6807-7-8
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Julkaisun pysyvä osoite on
https://urn.fi/urn:nbn:uta-3-612

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BioMed Central Open access
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Background

The chicken genome contains a BBP-A gene showing similar characteristics to avidin family genes. In a previous study we reported that the BBP-A gene may encode a biotin-binding protein due to the high sequence similarity with chicken avidin, especially at regions encoding residues known to be located at the ligand-binding site of avidin.

Results

Here, we expand the repertoire of known macromolecular biotin binders by reporting a novel biotin-binding protein A (BBP-A) from chicken. The BBP-A recombinant protein was expressed using two different expression systems and purified with affinity chromatography, biochemically characterized and two X-ray structures were solved – in complex with D-biotin (BTN) and in complex with D-biotin D-sulfoxide (BSO). The BBP-A protein binds free biotin with high, "streptavidin-like" affinity (Kd ~ 10-13 M), which is about 50 times lower than that of chicken avidin. Surprisingly, the affinity of BBP-A for BSO is even higher than the affinity for BTN. Furthermore, the solved structures of the BBP-A – BTN and BBP-A – BSO complexes, which share the fold with the members of the avidin and lipocalin protein families, are extremely similar to each other.

Conclusion

BBP-A is an avidin-like protein having a β-barrel fold and high affinity towards BTN. However, BBP-A differs from the other known members of the avidin protein family in thermal stability and immunological properties. BBP-A also has a unique ligand-binding property, the ability to bind BTN and BSO at comparable affinities. BBP-A may have use as a novel material in, e.g. modern bio(nano)technological applications.
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Kalevantie 5
PL 617
33014 Tampereen yliopisto
oa[@]tuni.fi | Tietosuoja | Saavutettavuusseloste