Structure of the Mtb CarD/RNAP β-lobes complex reveals the molecular basis of interaction and presents a distinct DNA-binding domain for Mtb CarD.
Structure of the Mtb CarD/RNAP β-lobes complex reveals the molecular basis of interaction and presents a distinct DNA-binding domain for Mtb CarD.
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DOI：
10.1016/j.str.2013.08.014
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发表时间：
2013-10-08
期刊：
影响因子：
5.7
通讯作者：
Sacchettini, James C.
中科院分区：
文献类型：
--
作者：
Gulten, Gulcin;Sacchettini, James C.
来自结核分枝杆菌（Mycobacterium tuberculosis，Mtb）的CardD是一种必需蛋白，被认为通过下调rRNA和核糖体蛋白基因参与严格应答。CardD与RNAP的β-亚基相互作用，这种相互作用对于Mtb在持续感染状态期间的存活至关重要。我们在2.1 nm分辨率下测定了与RNAP β亚基β1和β2结构域复合的CardD的晶体结构。该结构揭示了CardD/RNAP相互作用的分子基础，为进一步理解CardD对RNAP的调控提供了基础。CardD N-末端结构域的结构折叠在RNAP相互作用蛋白（如TRCF-RID和CdnL）中是保守的，并显示出与基于TRCF/RNAP β1结构预测的同源性模型相似的相互作用。有趣的是，C-末端结构域的结构，这是所需的完整的CardD功能在体内，代表了一种新的DNA结合折叠。
CarD from Mycobacterium tuberculosis (Mtb) is an essential protein thought to be involved in stringent response through downregulation of rRNA and ribosomal protein genes. CarD interacts with the β-subunit of RNAP and this interaction is vital for Mtb’s survival during the persistent infection state. We have determined the crystal structure of CarD in complex with the RNAP β-subunit β1 and β2 domains at 2.1 Å resolution. The structure reveals the molecular basis of CarD/RNAP interaction, providing a basis to further our understanding of RNAP regulation by CarD. The structural fold of the CarD N-terminal domain is conserved in RNAP interacting proteins such as TRCF-RID and CdnL, and displays similar interactions to the predicted homology model based on the TRCF/RNAP β1 structure. Interestingly, the structure of the C-terminal domain, which is required for complete CarD function in vivo, represents a novel DNA binding fold.
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影响因子：
4.8
作者：
Nechaev, S;Chlenov, M;Severinov, K
通讯作者：
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DOI：
10.1107/s0907444909052925
发表时间：
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期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
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影响因子：
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作者：
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