Structural characterization of GntR/HutC family signaling domain
Structural characterization of GntR/HutC family signaling domain
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DOI：
10.1110/ps.062146906
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发表时间：
2006-06-01
期刊：
影响因子：
8
通讯作者：
Savchenko, Alexei
中科院分区：
文献类型：
--
作者：
Gorelik, Marina;Lunin, Vladimir V.;Savchenko, Alexei
采用单波长异常色散（SAD）方法在1.7埃分辨率下解析了大肠杆菌PhnF c -末端结构域（C-PhnF）的晶体结构。PhnF蛋白属于大GntR转录调节因子家族的HutC亚家族。该家族的成员具有相似的n端dna结合域，但根据其异质的c端结构域分为四个亚家族，这些亚家族参与了效应结合和寡聚化。C-PhnF结构首次为HutC亚家族提供了该结构域的支架，HutC亚家族覆盖了约31%的gnr样调节因子。这种结构是螺旋和链的混合物，核心是六股反平行的链。C-PhnF单体通过建立域间八链β -片形成二聚体，其中包括每个单体的核心反平行和n端两链平行β -片。C-PhnF与choris酸裂解酶折叠具有很强的结构相似性，其特征是隐藏的活性位点锁定在两个螺旋-螺旋-螺旋环之后。C-PhnF和UbiC蛋白的结构比较使我们提出PhnF结构中类似的位点适合于效应物结合。
The crystal structure of Escherichia coli PhnF C-terminal domain (C-PhnF) was solved at 1.7 angstrom resolution by the single wavelength anomalous dispersion ( SAD) method. The PhnF protein belongs to the HutC subfamily of the large GntR transcriptional regulator family. Members of this family share similar N-terminal DNA-binding domains, but are divided into four subfamilies according to their heterogenic C-terminal domains, which are involved in effector binding and oligomerization. The C-PhnF structure provides for the first time the scaffold of this domain for the HutC subfamily, which covers about 31% of GntR-like regulators. The structure represents a mixture of alpha-helices and beta-strands, with a six-stranded antiparallel beta-sheet at the core. C-PhnF monomers form a dimer by establishing interdomain eight-strand beta-sheets that include core antiparallel and N-terminal two-strand parallel beta-sheets from each monomer. C-PhnF shares strong structural similarity with the chorismate lyase fold, which features a buried active site locked behind two helix-turn-helix loops. The structural comparison of the C-PhnF and UbiC proteins allows us to propose that a similar site in the PhnF structure is adapted for effector binding.