PF0610, a novel winged helix-turn-helix variant possessing a rubredoxin-like Zn ribbon motif from the hyperthermophilic archaeon, Pyrococcus furiosus.

PF0610, a novel winged helix-turn-helix variant possessing a rubredoxin-like Zn ribbon motif from the hyperthermophilic archaeon, Pyrococcus furiosus.
复制标题

PF0610,一种新型有翼螺旋-转角-螺旋变体,具有来自超嗜热古菌激烈火球菌的红氧还蛋白样锌带基序。

DOI:
10.1021/bi061870h
复制
发表时间:
2007
期刊:
影响因子:
2.9
通讯作者:
Prestegard,JamesH
Prestegard,JamesH
中科院分区:
生物学3区
文献类型:
--
作者:
Wang,Xu;Lee,Han-Seung;Sugar,FrankJ;JenneyJr,FrancisE;Adams,MichaelWW;Prestegard,JamesH

文献摘要

被引文献

相似文献

PF 0610是一种来自极端嗜热菌Pyrococcus furiosus的蛋白质,仅在其他古细菌物种和三种Fe(III)还原细菌中具有同源物。它被认为在N-末端有一个螺旋-转角-螺旋(HTH)结构域,并具有两个金属结合蛋白特有的CXXC基序。我们已经确定了溶液结构的锌结合蛋白质使用NMR。PF 0610是一种新型带翼螺旋-转角-螺旋(wHTH)蛋白,其W1片段为红氧蛋白样锌带。此外,它在其表面上具有大量的碱性残基。在螺旋H3和W1的金属结合环上都可以发现碱性残基簇,这表明它可能是一种DNA结合蛋白。因此,使用线性和环状DNA的凝胶位移测定显示PF 0610确实结合DNA,至少以序列非依赖性方式。基于其他wHTH蛋白-DNA结构的PF 0610-DNA相互作用模型显示,除了螺旋H3之外,金属结合环中第二个CXXC基序周围的碱性残基可以与DNA进行广泛的接触。然而,W1区域的庞大性意味着DNA构象可能在PF 0610结合时发生扭曲。PF 0610是已知的第一个具有Zn带嵌入的wHTH折叠的蛋白质,因此,具有作为金属依赖性转录调节因子和作为染色体包装系统inP的组分的潜在作用。愤怒这一新结构的发现代表了有翼HTH蛋白家族的又一个分支,有助于我们理解P的转录调控过程。愤怒
PF0610, a protein from the hyperthermophilePyrococcus furiosus, has homologues only in other archaeal species and in three species of Fe(III)-reducing bacteria. It is thought to have a helix−turn−helix (HTH) domain at the N-terminus and possesses two CXXC motifs characteristic of metal binding proteins. We have determined the solution structure of the Zn-bound protein using NMR. PF0610 is a novel winged helix−turn−helix (wHTH) protein with a rubredoxin-like Zn ribbon as its W1 segment. In addition, it possesses a large number of basic residues on its surface. Clusters of basic residues can be found on both helix H3 and the metal-binding loops of W1, suggesting that it might be a DNA-binding protein. Accordingly, gel shift assays using both linear and circular DNA showed that PF0610 does bind DNA, at least in a sequence-independent fashion. Modeling the PF0610−DNA interaction based on other wHTH protein−DNA structures revealed that besides helix H3, basic residues around the second CXXC motif in the metal-binding loop could make extensive contacts with DNA. However, the bulkiness of the W1 region implies that the DNA conformation may be distorted upon PF0610 binding. PF0610 is the first protein known to have a Zn ribbon-embedded wHTH fold and, as such, has potential roles both as a metal-dependent transcription regulator and as a component of the chromosome packing system inP. furiosus. The discovery of this novel structure represents the addition of another branch to the winged HTH protein family and could contribute to our understanding of transcription regulatory processes inP. furiosus.