Structure and characterization of a novel chicken biotin-binding protein A (BBP-A).
Structure and characterization of a novel chicken biotin-binding protein A (BBP-A).
复制标题
DOI：
10.1186/1472-6807-7-8
复制
发表时间：
2007-03-07
影响因子：
--
通讯作者：
Airenne TT
中科院分区：
文献类型：
--
作者：
Hytönen VP;Määttä JA;Niskanen EA;Huuskonen J;Helttunen KJ;Halling KK;Nordlund HR;Rissanen K;Johnson MS;Salminen TA;Kulomaa MS;Laitinen OH;Airenne TT
鸡的基因组包含一个BBP-A基因，显示出与亲和素家族基因相似的特征。在以前的研究中，我们报道了BBP-A基因可能编码一个生物素结合蛋白，因为它与鸡亲和素有很高的序列相似性，特别是在已知的位于亲和素配体结合位点的编码残基的区域。在这里，我们通过报道一种来自鸡的新的生物素结合蛋白A(BBP-A)来扩展已知的大分子生物素结合蛋白的谱系。用两种不同的表达系统表达了BBP-A重组蛋白，并用亲和层析对其进行了纯化，对重组蛋白进行了生化鉴定和两种X射线结构的解析--与D-生物素(BTN)和与D-生物素(BSO)的络合物。BBP-A蛋白与游离生物素的结合具有很高的类链霉亲和素亲和力(Kd~10-13M)，比鸡亲和素的亲和力低约50倍。令人惊讶的是，BBP-A对BSO的亲和力甚至高于对BTN的亲和力。此外，BBP-A-BTN和BBP-A-BSO与亲和素和Lipocalin蛋白家族成员共享折叠的BBP-A-BTN和BBP-A-BSO复合物的溶解结构非常相似。BBP-A是一种亲和素样蛋白，具有β桶折叠，与Btn有很高的亲和力。然而，BBP-A在热稳定性和免疫学性质上不同于亲和素家族的其他已知成员。BBP-A还具有独特的配体结合特性，能够以类似的亲和力结合BTN和BSO。BBP-A可能在现代生物(纳米)技术应用中用作一种新材料。
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. 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. 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.
登录
查看更多内容
影响因子：
4
作者：
BOTTE, V;GRANATA, G
通讯作者：
GRANATA, G
影响因子：
4.1
作者：
BUSH, L;MCGAHAN, TJ;WHITE, HB
通讯作者：
WHITE, HB
DOI：
10.1107/s0907444905003914
发表时间：
2005-05-01
影响因子：
2.2
作者：
Eisenberg-Domovich, Y;Hytönen, VP;Livnah, O
通讯作者：
Livnah, O
影响因子：
4.8
作者：
Hytönen, VP;Nyholm, TKM;Kulomaa, MS
通讯作者：
Kulomaa, MS
影响因子：
15
作者：
DETITTA, GT;EDMONDS, JW;DONOHUE, J
通讯作者：
DONOHUE, J