Bacillus licheniformis Anti-TRAP can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers.

Bacillus licheniformis Anti-TRAP can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers.
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DOI:
10.1016/j.jsb.2010.01.013
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发表时间:
2010-04
影响因子:
3
通讯作者:
Antson, Alfred A.
Antson, Alfred A.
中科院分区:
生物学3区
文献类型:
--
作者:
Shevtsov, Mikhail B.;Chen, Yanling;Isupov, Michail N.;Leech, Andrew;Gollnick, Paul;Antson, Alfred A.

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抗TRAP(AT)蛋白通过与trp RNA结合衰减蛋白(TRAP)结合并阻止其与RNA相互作用来调节色氨酸生物合成基因的表达。枯草芽孢杆菌AT形成可与TRAP相互作用或可进一步组装成十二聚体颗粒的三聚体。为了确定其他杆菌的AT蛋白中保留了哪些寡聚形式,我们研究了地衣芽孢杆菌AT,它与B有66%的序列同一性。枯草杆菌蛋白我们证明了在溶液B中。地衣AT形成稳定的三聚体。在晶体中,根据pH值,这种三聚体组装成两种不同类型的十二聚体颗粒,两者都具有23点群对称性。在pH 6.0下形成的十二聚体具有与先前观察到的B相同的构象。枯草芽孢杆菌这个十二聚体包含一个体积为10700立方厘米的大内腔,里面排列着十二个缬氨酸残基的侧链。疏水室的存在暗示了通过配体的结合可以诱导十二聚体形成的可能性。有趣的是,在pH 8.0下形成的十二聚体中,相对于在pH 6.0下观察到的形式,所有三聚体都被翻转。
Anti-TRAP (AT) protein regulates expression of tryptophan biosynthetic genes by binding to the trp RNA-binding attenuation protein (TRAP) and preventing its interaction with RNA. Bacillus subtilis AT forms trimers that can either interact with TRAP or can further assemble into dodecameric particles. To determine which oligomeric forms are preserved in AT proteins of other Bacilli we studied Bacillus licheniformis AT which shares 66% sequence identity with the B. subtilis protein. We show that in solution B. licheniformis AT forms stable trimers. In crystals, depending on pH, such trimers assemble into two different types of dodecameric particles, both having 23 point group symmetry. The dodecamer formed at pH 6.0 has the same conformation as previously observed for B. subtilis AT. This dodecamer contains a large internal chamber with the volume of ∼700 Å3, which is lined by the side chains of twelve valine residues. The presence of the hydrophobic chamber hints at the possibility that the dodecamer formation could be induced by binding of a ligand. Interestingly, in the dodecamer formed at pH 8.0 all trimers are turned inside out relatively to the form observed at pH 6.0.
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