STRUCTURAL STUDIES OF THE PHOQ SENSOR DOMAIN

PHOQ 传感器领域的结构研究

• 批准号: 7721639
• 负责人: PONNI RAJAGOPAL
• 金额: $ 0.28万
• 依托单位: UNIVERSITY OF WISCONSIN-MADISON
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-03-01 至 2009-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7721639
• 关键词: Antimicrobial Resistance; Binding; Computer Retrieval of Information on Scientific Projects Database; Condition; Cues; Divalent Cations; Funding; Grant; Institution; Membrane; Molecular; Phosphotransferases; Play; Process; Repression; Research; Research Personnel; Resources; Role; Signal Transduction; Source; Structure; System; United States National Institutes of Health; Virulence; antimicrobial peptide; interest; periplasm; sensor

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The two-component regulatory system PhoPQ plays a central role in resistance to antimicrobial peptides and bacterial virulence. The PhoQ periplasmic sensor domain is essential for the activation and repression of PhoQ's kinase activity through its ability to sense environmental cues. There is strong evidence that divalent cations (Ca++ and Mg++) repress activation of PhoPQ by binding to the periplasmic domain of PhoQ. This binding likely induces a conformational change that is believed to transmit through the bacterial membrane, repressing activity of the PhoQ kinase domain responsible for induction of PhoP and further downstream processes. We are interested in the molecular mechanism of signal sensing and are investigating the structure of the sensor domain under varied environmental conditions.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 两个组分的调节系统PHOPQ在抗菌肽和细菌毒力的耐药性中起着核心作用。 Phoq Pariplasmic传感器结构域对于通过感知环境提示的能力来激活和抑制Phoq的激酶活性至关重要。有充分的证据表明，二价阳离子（Ca ++和Mg ++）通过与Phoq的周质结构域结合来抑制PhOPQ。这种结合可能会引起构象变化，该构象变化被认为通过细菌膜传播，抑制了负责诱导PHOP和进一步下游过程的Phoq激酶域的活性。我们对信号传感的分子机制感兴趣，并正在研究各种环境条件下传感器结构域的结构。