NMR structure of AbhN and comparison with AbrBN - First insights into the DNA binding promiscuity and specificity of AbrB-like transition state regulator proteins
NMR structure of AbhN and comparison with AbrBN - First insights into the DNA binding promiscuity and specificity of AbrB-like transition state regulator proteins
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DOI：
10.1074/jbc.m601963200
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发表时间：
2006-07-28
影响因子：
4.8
通讯作者：
Cavanagh, John
中科院分区：
文献类型：
--
作者：
Bobay, Benjamin G.;Mueller, Geoffrey A.;Cavanagh, John
了解过渡态调节蛋白的分子机制至关重要，因为它们在细菌科普不断变化的环境的能力中发挥着关键作用。虽然很多努力都集中在他们的遗传特性，很少有人知道他们的结构和功能的保护。在这里，我们提出了高分辨率的NMR溶液结构的N-末端结构域的枯草芽孢杆菌过渡态调节剂ABH（AbhN），只有第二个这样的结构到目前为止。然后我们将AbhN与B的N-末端DNA结合结构域进行比较。枯草杆菌AbrB（AbrBN）。这是两个类似AbrB的过渡态调节器之间的第一次这样的比较。AbhN和AbrBN非常相似，表明它们的DNA结合具有共同的结构基础。然而，我们也注意到AbhN和AbrBN结构之间的细微差异，这可能在DNA靶特异性中发挥重要作用。伴随的体外DNA结合研究的结果突出了两种蛋白质之间的结合差异。
Understanding the molecular mechanisms of transition state regulator proteins is critical, since they play a pivotal role in the ability of bacteria to cope with changing environments. Although much effort has focused on their genetic characterization, little is known about their structural and functional conservation. Here we present the high resolution NMR solution structure of the N-terminal domain of the Bacillus subtilis transition state regulator Abh (AbhN), only the second such structure to date. We then compare AbhN to the N-terminal DNA-binding domain of B. subtilis AbrB (AbrBN). This is the first such comparison between two AbrB-like transition state regulators. AbhN and AbrBN are very similar, suggesting a common structural basis for their DNA binding. However, we also note subtle variances between the AbhN and AbrBN structures, which may play important roles in DNA target specificity. The results of accompanying in vitro DNA-binding studies serve to highlight binding differences between the two proteins.