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创伤弧菌转录激活因子 HlyU 的晶体结构

Crystal structure of the transcriptional activator HlyU from Vibrio vulnificus CMCP6.

机构信息

Department of Chemistry, Chonnam National University, Gwangju, Republic of Korea.

出版信息

FEBS Lett. 2010 Mar 19;584(6):1097-102. doi: 10.1016/j.febslet.2010.02.052. Epub 2010 Feb 21.

Abstract

HlyU is a transcription factor of the ArsR/SmtB family and activates the expression of the pathogenic Vibrio vulnificus RTX toxin. In contrast to the other metal-responding ArsR/SmtB proteins, HlyU does not sense metal ions. To provide its structural information, we elucidated the crystal structure of HlyU from V. vulnificus CMCP6 (HlyU_Vv). The monomeric HlyU_Vv architecture of five alpha-helices and two beta-strands, some of which constitute a typical DNA-binding winged helix-turn-helix (wHTH) motif, is very similar to that of other transcription regulators. Nonetheless, the homo-dimeric HlyU_Vv structure shows several different, three-dimensional features in the spatial position and the detailed dimeric interaction, which were not observed in the modeling study based on the same protein family and sequence similarity.

摘要

HlyU 是 ArsR/SmtB 家族的转录因子,可激活致病性创伤弧菌 RTX 毒素的表达。与其他金属响应 ArsR/SmtB 蛋白不同,HlyU 不感应金属离子。为了提供其结构信息,我们解析了来自创伤弧菌 CMCP6(HlyU_Vv)的 HlyU 的晶体结构。单体 HlyU_Vv 由五个α-螺旋和两个β-链组成,其中一些构成了典型的 DNA 结合翼型螺旋-转角-螺旋(wHTH)基序,与其他转录调节剂非常相似。然而,同源二聚体 HlyU_Vv 结构在空间位置和详细的二聚体相互作用方面表现出几个不同的三维特征,这些特征在基于相同蛋白质家族和序列相似性的建模研究中没有观察到。

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