Crystal structure of a histidine kinase sensor domain with similarity to periplasmic binding proteins.
Crystal structure of a histidine kinase sensor domain with similarity to periplasmic binding proteins.
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DOI：
10.1002/prot.22485
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发表时间：
2009-10
影响因子：
2.9
通讯作者：
Hendrickson, Wayne A.
中科院分区：
文献类型：
--
作者：
Cheung, Jonah;Le-Khac, Matthew;Hendrickson, Wayne A.
组氨酸激酶受体是细菌和低等真核生物中常见的双组分信号转导系统的组成部分，它们通过细胞外变化与细胞内反应的耦合对环境适应至关重要1，2。典型的双组分系统由跨膜组氨酸激酶传感器和细胞质反应调节剂组成。在经典系统中，细胞外信号，如小分子配体和离子检测的组氨酸激酶受体的周质传感器结构域，其调节细胞质组氨酸激酶结构域的催化活性，并促进ATP依赖性的保守的组氨酸残基的自磷酸化。磷酸盐随后通过磷酸转移机制转移到同源反应调节剂的保守天冬氨酸，并且依次调节反应调节剂的活性3，4。组氨酸激酶传感器蛋白的催化结构域和其他细胞质元件是保守的，而传感器结构域是模块化的，序列高度可变。数以千计的组氨酸激酶已被确定通过基因组测序计划，但其中许多仍然生化未确定。作为一个结构基因组学项目的一部分，旨在了解所有已知的传感器域之间的结构关系，我们已经解决了一个以前未表征的传感器域的结构，从组氨酸激酶蛋白编码的Gesophylsulfreducens GSU2755基因，最初确定和注释通过基因组测序的organism5。我们使用名称HK29来表示这个假定的传感器域。该结构揭示了一个以前未表征的组氨酸激酶传感器结构域折叠。
Histidine kinase receptors are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes, where they are crucial for environmental adaptation through the coupling of extracellular changes to intracellular responses1, 2. The typical two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. In the classic system, extracellular signals such as small molecule ligands and ions are detected by the periplasmic sensor domain of the histidine kinase receptor which modulates the catalytic activity of the cytoplasmic histidine kinase domain and promotes ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is subsequently transferred to a conserved aspartate of the cognate response regulator through a phosphotransfer mechanism, and the activity of the response regulator is modulated in turn3, 4. The response regulator often controls gene transcription or flagellar rotation, and thus allows cellular adaptation to an environmental signal.The nature of histidine kinase sensor proteins is such that the catalytic domain and other cytoplasmic elements are conserved whereas the sensor domains are modular and highly variable in sequence. Thousands of histidine kinases have been identified through genome sequencing projects, but many of these remain biochemically uncharacterized. As part of a structural genomics project aimed at understanding the structural relationships between all known sensor domains, we have solved the structure of a previously uncharacterized sensor domain from a histidine kinase protein encoded by the Geobacter sulfurreducens GSU2755 gene, originally identified and annotated through genome sequencing of the organism5. We use the name HK29s to for this putative sensor domain. The structure reveals a previously uncharacterized histidine kinase sensor domain fold.
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影响因子：
56.9
作者：
Methé, BA;Nelson, KE;Fraser, CM
通讯作者：
Fraser, CM
PHOQ传感器结构域功能二聚体的晶体结构。
影响因子：
4.8
作者：
Cheung, Jonah;Bingman, Craig A.;Reyngold, Marsha;Hendrickson, Wayne A.;Waldburger, Carey D.
通讯作者：
Waldburger, Carey D.
DOI：
10.1107/s0907444998003254
发表时间：
1998-09-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
Brunger, AT;Adams, PD;Warren, GL
通讯作者：
Warren, GL
影响因子：
2.9
作者：
CAREAGA, CL;SUTHERLAND, J;FALKE, JJ
通讯作者：
FALKE, JJ
影响因子：
3.6
作者：
Müller, A;Thomas, GH;Wilkinson, AJ
通讯作者：
Wilkinson, AJ