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

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Show simple item record Hytönen, Vesa P. Määttä, Juha A. E. Niskanen, Einari A. Huuskonen, Juhani Helttunen, Kaisa J. Halling, Katrin K. Nordlund, Henri R. Rissanen, Kari Johnson, Mark S. Salminen, Tiina A. Kulomaa, Markku S. Laitinen, Olli H. Airenne, Tomi T. 2012-11-22T07:03:10Z 2012-11-22T07:03:10Z 2007 fi
dc.identifier.citation 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. fi
dc.identifier.issn 1472-6807
dc.description.abstract 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. fi
dc.language.iso eng
dc.publisher BioMed Central (BMC)
dc.relation.ispartofseries BMC Structural Biology
dc.rights © 2007 Hytönen et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
dc.rights openAccess fi
dc.subject.other biotiini fi
dc.subject.other kiderakenne
dc.subject.other biotin
dc.subject.other x-ray structure
dc.title Structure and characterization of a novel chicken biotin-binding protein A (BBP-A)
dc.type Article
dc.identifier.urn URN:NBN:fi:jyu-201804202289
dc.contributor.laitos Kemian laitos fi
dc.contributor.laitos Department of Chemistry en
dc.identifier.doi 10.1186/1472-6807-7-8 2012-11-15T14:55:10Z
dc.description.version Publisher's PDF
dc.type.coar journal article
dc.description.reviewstatus peerReviewed
dc.relation.issn 1472-6807
dc.type.version publishedVersion

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