STRUCTURAL STUDIES OF BACTERIAL PROTEIN COMPLEXES

细菌蛋白复合物的结构研究

• 批准号: 8170085
• 负责人: Liang Tang
• 金额: $ 0.64万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-05-01 至 2011-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8170085
• 关键词: Bacterial Proteins; Cell membrane; Computer Retrieval of Information on Scientific Projects Database; Cytoplasm; Drug Design; Drug resistance; Funding; Grant; Institution; Membrane; Molecular; Molecular Chaperones; Protein Secretion; Protein translocation; Proteins; Research; Research Personnel; Resources; Shigella; Signal Transduction; Source; Structure; Type III Secretion System Pathway; United States National Institutes of Health; pathogenic bacteria; protein complex; protein-histidine kinase

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. Many Gram-negative pathogenic bacteria employ a sophisticated protein secretion apparatus termed type III secretion system (T3SS) to transport bacterial effector proteins into eukaryotic host cytoplasm. The translocon, a structural component of T3SS, is a protein complex that traverses the host cell membrane for translocation of effector proteins. The molecular mechanisms underlying the T3SS protein translocation remain unclear. Our research is focused on the structures of Shigella translocon proteins IpaB and IpaC and their chaperone IpgC. IpgC single crystals have been obtained and optimization is underway. Histidine kinases have been attractive new targets for drug design to circumvent drug resistance in Grampositive pathogenic bacteria. Our research is aimed at structure and function of a multidomainal, membrane spanning histidine kinase from an essential two-component signal transduction system.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 许多革兰氏阴性病原菌利用称为III型分泌系统（T3 SS）的复杂蛋白分泌装置将细菌效应蛋白转运到真核宿主细胞质中。易位子是T3 SS的结构组分，是穿过宿主细胞膜用于效应蛋白易位的蛋白质复合物。T3 SS蛋白转位的分子机制尚不清楚。我们的研究主要集中在志贺菌易位蛋白IpaB和IpaC及其伴侣IpgC的结构上。已经获得IpgC单晶，并且正在进行优化。组氨酸激酶已成为药物设计的有吸引力的新靶点，以规避革兰氏阳性病原菌的耐药性。我们的研究是针对一个多域，跨膜组氨酸激酶的结构和功能，从一个重要的双组分信号转导系统。