Structure and characterization of a novel chicken biotin-binding protein A (BBP-A)
Downloads:
Rissanen, K., Huuskonen, J., Määttä, J., Niskanen, E., Helttunen, K., Halling, K., Slotte, J. P., Nordlund, H., Johnson, M., Salminen, T., Kulomaa, M., Laitinen, O. Airenne, T. & Hytönen, V. (2007). Structure and characterization of a novel chicken biotin-binding protein A (BBP-A). BMC Structural Biology, , 8 - 15.
Published in
BMC Structural BiologyAuthors
Date
2007Copyright
© 2007 Hytönen et al; licensee BioMed Central Ltd.
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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.
...
Publisher
BioMed Central (BMC)ISSN Search the Publication Forum
1472-6807Keywords
Metadata
Show full item recordCollections
License
Except where otherwise noted, this item's license is described as © 2007 Hytönen et al; licensee BioMed Central Ltd.
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Related items
Showing items with similar title or keywords.
-
Chicken genome analysis reveals novel genes encoding biotin-binding proteins related to avidin family
Niskanen, Einari A; Hytönen, Vesa P; Grapputo, Alessandro; Nordlund, Henri R; Kulomaa, Markku S; Laitinen, Olli H (BioMed Central (BMC), 2005)Background A chicken egg contains several biotin-binding proteins (BBPs), whose complete DNA and amino acid sequences are not known. In order to identify and characterise these genes and ... -
The avidin protein family : properties of family members and engineering of novel biotin-binding protein tools
Hytönen, Vesa (University of Jyväskylä, 2005)Eliöiden perimä sisältää kullekin lajille tyypillisen geneettisen tiedon ja määrittelee niiden ominaisuuksia. Lajien perimän yksityiskohtainen tarkastelu ja vertailu selvittää lajien ominaisuuksien perustaa. Suuri osa ... -
Rational drug discovery : structural studies of protein-ligand complexes
Nurminen, Elisa (University of Jyväskylä, 2011) -
Structural insight of PP2A inhibitor proteins and their interaction with PP2A Aand B56-subunits
Thapa, Chandan Jung (Jyväskylän yliopisto, 2021)Protein phosphatase 2A (PP2A), the principal Serine/Threonine phosphatase, functions as a tumor suppressor. In most of the cancers, the PP2A tumor suppressor activity is inhibited either genetically or by the overexpression ...